메뉴 건너뛰기




Volumn 92, Issue 3, 2011, Pages 389-407

Nanobodies¯: New ammunition to battle viruses

Author keywords

Antiviral; Camelidae; Heavy chain only antibody; Nanobody; VHH

Indexed keywords

CHEMOKINE RECEPTOR CXCR4; GLYCOPROTEIN GP 120; NANOBODY; NUCLEOCAPSID PROTEIN;

EID: 80355141486     PISSN: 01663542     EISSN: 18729096     Source Type: Journal    
DOI: 10.1016/j.antiviral.2011.09.002     Document Type: Review
Times cited : (122)

References (155)
  • 7
    • 33846502163 scopus 로고    scopus 로고
    • Hepatitis B virus morphogenesis
    • Bruss, V., Hepatitis B virus morphogenesis. World J. Gastroenterol. 13 (2007), 65–73.
    • (2007) World J. Gastroenterol. , vol.13 , pp. 65-73
    • Bruss, V.1
  • 9
    • 0029962378 scopus 로고    scopus 로고
    • Protective effect of rotavirus VP6-specific IgA monoclonal antibodies that lack neutralizing activity
    • Burns, J.W., Siadat-Pajouh, M., Krishnaney, A.A., Greenberg, H.B., Protective effect of rotavirus VP6-specific IgA monoclonal antibodies that lack neutralizing activity. Science 272 (1996), 104–107.
    • (1996) Science , vol.272 , pp. 104-107
    • Burns, J.W.1    Siadat-Pajouh, M.2    Krishnaney, A.A.3    Greenberg, H.B.4
  • 10
    • 0025838698 scopus 로고
    • A large array of human monoclonal antibodies to type 1 human immunodeficiency virus from combinatorial libraries of asymptomatic seropositive individuals
    • Burton, D.R., Barbas, C.F. 3rd, Persson, M.A., Koenig, S., Chanock, R.M., Lerner, R.A., A large array of human monoclonal antibodies to type 1 human immunodeficiency virus from combinatorial libraries of asymptomatic seropositive individuals. Proc. Natl. Acad. Sci. USA 88 (1991), 10134–10137.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10134-10137
    • Burton, D.R.1    Barbas, C.F.2    Persson, M.A.3    Koenig, S.4    Chanock, R.M.5    Lerner, R.A.6
  • 12
    • 0343618590 scopus 로고    scopus 로고
    • Electron microscopy of the human respiratory syncytial virus fusion protein and complexes that it forms with monoclonal antibodies
    • Calder, L.J., González-Reyes, L., García-Barreno, B., Wharton, S.A., Skehel, J.J., Wiley, D.C., Melero, J.A., Electron microscopy of the human respiratory syncytial virus fusion protein and complexes that it forms with monoclonal antibodies. Virology 271 (2000), 122–131.
    • (2000) Virology , vol.271 , pp. 122-131
    • Calder, L.J.1    González-Reyes, L.2    García-Barreno, B.3    Wharton, S.A.4    Skehel, J.J.5    Wiley, D.C.6    Melero, J.A.7
  • 14
    • 0035831483 scopus 로고    scopus 로고
    • Camel single-domain antibodies as modular building units in bispecific and bivalent antibody constructs
    • Conrath, K., Lauwereys, M., Wyns, L., Muyldermans, S., Camel single-domain antibodies as modular building units in bispecific and bivalent antibody constructs. J. Biol. Chem. 276 (2001), 7346–7350.
    • (2001) J. Biol. Chem. , vol.276 , pp. 7346-7350
    • Conrath, K.1    Lauwereys, M.2    Wyns, L.3    Muyldermans, S.4
  • 17
    • 33750358221 scopus 로고    scopus 로고
    • Rotavirus anti-VP6 secretory immunoglobulin A contributes to protection via intracellular neutralization but not via immune exclusion
    • Corthésy, B., Benureau, Y., Perrier, C., Fourgeux, C., Parez, N., Greenberg, H., Schwartz-Cornil, I., Rotavirus anti-VP6 secretory immunoglobulin A contributes to protection via intracellular neutralization but not via immune exclusion. J. Virol. 80 (2006), 10692–10699.
    • (2006) J. Virol. , vol.80 , pp. 10692-10699
    • Corthésy, B.1    Benureau, Y.2    Perrier, C.3    Fourgeux, C.4    Parez, N.5    Greenberg, H.6    Schwartz-Cornil, I.7
  • 18
    • 0034000469 scopus 로고    scopus 로고
    • Establishment and characterization of molecular clones of porcine endogenous retroviruses replicating on human cells
    • Czauderna, F., Fischer, N., Boller, K., Kurth, R., Tönjes, R.R., Establishment and characterization of molecular clones of porcine endogenous retroviruses replicating on human cells. J. Virol. 74 (2000), 4028–4038.
    • (2000) J. Virol. , vol.74 , pp. 4028-4038
    • Czauderna, F.1    Fischer, N.2    Boller, K.3    Kurth, R.4    Tönjes, R.R.5
  • 19
    • 11844272621 scopus 로고    scopus 로고
    • Kinetic and molecular analysis of nuclear export factor CRM1 association with its cargo in vivo
    • Daelemans, D., Costes, S.V., Lockett, S., Pavlakis, G.N., Kinetic and molecular analysis of nuclear export factor CRM1 association with its cargo in vivo. Mol. Cell. Biol. 25 (2005), 728–739.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 728-739
    • Daelemans, D.1    Costes, S.V.2    Lockett, S.3    Pavlakis, G.N.4
  • 23
  • 24
    • 0242300184 scopus 로고    scopus 로고
    • Intracellularly expressed single-domain antibody against p15 matrix protein prevents the production of porcine retroviruses
    • Dekker, S., Toussaint, W., Panayotou, G., de Wit, T., Visser, P., Grosveld, F., Drabek, D., Intracellularly expressed single-domain antibody against p15 matrix protein prevents the production of porcine retroviruses. J. Virol. 77 (2003), 12132–12139.
    • (2003) J. Virol. , vol.77 , pp. 12132-12139
    • Dekker, S.1    Toussaint, W.2    Panayotou, G.3    de Wit, T.4    Visser, P.5    Grosveld, F.6    Drabek, D.7
  • 25
    • 0034667748 scopus 로고    scopus 로고
    • Transmission of porcine endogenous retroviruses in severe combined immunodeficient mice xenotransplanted with fetal porcine pancreatic cells
    • Deng, Y.M., Tuch, B.E., Rawlinson, W.D., Transmission of porcine endogenous retroviruses in severe combined immunodeficient mice xenotransplanted with fetal porcine pancreatic cells. Transplantation 70 (2000), 1010–1016.
    • (2000) Transplantation , vol.70 , pp. 1010-1016
    • Deng, Y.M.1    Tuch, B.E.2    Rawlinson, W.D.3
  • 26
    • 79959762066 scopus 로고    scopus 로고
    • Infectious risk in xenotransplantation – what post-transplant screening for the human recipient?
    • Denner, J., Infectious risk in xenotransplantation – what post-transplant screening for the human recipient?. Xenotransplantation 18 (2011), 151–157.
    • (2011) Xenotransplantation , vol.18 , pp. 151-157
    • Denner, J.1
  • 27
    • 77954739350 scopus 로고    scopus 로고
    • A novel promiscuous class of camelid single-domain antibody contributes to the antigen-binding repertoire
    • Deschacht, N., De Groeve, K., Vincke, C., Raes, G., De Baetselier, P., Muyldermans, S., A novel promiscuous class of camelid single-domain antibody contributes to the antigen-binding repertoire. J. Immunol. 184 (2010), 5696–5704.
    • (2010) J. Immunol. , vol.184 , pp. 5696-5704
    • Deschacht, N.1    De Groeve, K.2    Vincke, C.3    Raes, G.4    De Baetselier, P.5    Muyldermans, S.6
  • 28
    • 0035854724 scopus 로고    scopus 로고
    • Antigen specificity and high affinity binding provided by one single loop of a camel single-domain antibody
    • Desmyter, A., Decanniere, K., Muyldermans, S., Wyns, L., Antigen specificity and high affinity binding provided by one single loop of a camel single-domain antibody. J. Biol. Chem. 276 (2001), 26285–26290.
    • (2001) J. Biol. Chem. , vol.276 , pp. 26285-26290
    • Desmyter, A.1    Decanniere, K.2    Muyldermans, S.3    Wyns, L.4
  • 32
    • 0037133506 scopus 로고    scopus 로고
    • Biophysical properties of camelid V(HH) domains compared to those of human V(H)3 domains
    • Ewert, S., Cambillau, C., Conrath, K., Plückthun, A., Biophysical properties of camelid V(HH) domains compared to those of human V(H)3 domains. Biochemistry 41 (2002), 3628–3636.
    • (2002) Biochemistry , vol.41 , pp. 3628-3636
    • Ewert, S.1    Cambillau, C.2    Conrath, K.3    Plückthun, A.4
  • 34
    • 0041822178 scopus 로고    scopus 로고
    • New targets and possible new therapeutic approaches in the chemotherapy of chronic hepatitis B
    • Feld, J., Lee, J.-yee, Locarnini, S., New targets and possible new therapeutic approaches in the chemotherapy of chronic hepatitis B. Hepatology 38 (2003), 545–553.
    • (2003) Hepatology , vol.38 , pp. 545-553
    • Feld, J.1    Lee, J.-Y.2    Locarnini, S.3
  • 35
    • 0029130169 scopus 로고
    • The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs
    • Fischer, U., Huber, J., Boelens, W.C., Mattaj, I.W., Lührmann, R., The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs. Cell 82 (1995), 475–483.
    • (1995) Cell , vol.82 , pp. 475-483
    • Fischer, U.1    Huber, J.2    Boelens, W.C.3    Mattaj, I.W.4    Lührmann, R.5
  • 36
    • 0030924190 scopus 로고    scopus 로고
    • CRM1 is an export receptor for leucine-rich nuclear export signals
    • Fornerod, M., Ohno, M., Yoshida, M., Mattaj, I.W., CRM1 is an export receptor for leucine-rich nuclear export signals. Cell 90 (1997), 1051–1060.
    • (1997) Cell , vol.90 , pp. 1051-1060
    • Fornerod, M.1    Ohno, M.2    Yoshida, M.3    Mattaj, I.W.4
  • 38
    • 53549119688 scopus 로고    scopus 로고
    • HIV-1 Nef: at the crossroads
    • Foster, J.L., Garcia, J.V., HIV-1 Nef: at the crossroads. Retrovirology, 5, 2008, 84.
    • (2008) Retrovirology , vol.5 , pp. 84
    • Foster, J.L.1    Garcia, J.V.2
  • 39
    • 0030831534 scopus 로고    scopus 로고
    • CRM1 is responsible for intracellular transport mediated by the nuclear export signal
    • Fukuda, M., Asano, S., Nakamura, T., Adachi, M., Yoshida, M., Yanagida, M., Nishida, E., CRM1 is responsible for intracellular transport mediated by the nuclear export signal. Nature 390 (1997), 308–311.
    • (1997) Nature , vol.390 , pp. 308-311
    • Fukuda, M.1    Asano, S.2    Nakamura, T.3    Adachi, M.4    Yoshida, M.5    Yanagida, M.6    Nishida, E.7
  • 40
    • 52649114833 scopus 로고    scopus 로고
    • Llama-derived single-chain antibody fragments directed to rotavirus VP6 protein possess broad neutralizing activity in vitro and confer protection against diarrhea in mice
    • Garaicoechea, L., Olichon, A., Marcoppido, G., Wigdorovitz, A., Mozgovoj, M., Saif, L., Surrey, T., Parreño, V., Llama-derived single-chain antibody fragments directed to rotavirus VP6 protein possess broad neutralizing activity in vitro and confer protection against diarrhea in mice. J. Virol. 82 (2008), 9753–9764.
    • (2008) J. Virol. , vol.82 , pp. 9753-9764
    • Garaicoechea, L.1    Olichon, A.2    Marcoppido, G.3    Wigdorovitz, A.4    Mozgovoj, M.5    Saif, L.6    Surrey, T.7    Parreño, V.8
  • 44
    • 0028962371 scopus 로고    scopus 로고
    • A new antigen receptor gene family that undergoes rearrangement and extensive somatic diversification in sharks
    • Greenberg, A.S., Avila, D., Hughes, M., McKinney, E.C., Flajnik, M.F., A new antigen receptor gene family that undergoes rearrangement and extensive somatic diversification in sharks. Nature 374 (1996), 168–173.
    • (1996) Nature , vol.374 , pp. 168-173
    • Greenberg, A.S.1    Avila, D.2    Hughes, M.3    McKinney, E.C.4    Flajnik, M.F.5
  • 46
    • 0027384670 scopus 로고
    • Prophylactic administration of respiratory syncytial virus immune globulin to high-risk infants and young children. The respiratory syncytial virus immune globulin study group
    • Groothuis, J.R., Simoes, E.A., Levin, M.J., Hall, C.B., Long, C.E., Rodriguez, W.J., Arrobio, J., Meissner, H.C., Fulton, D.R., Welliver, R.C., Prophylactic administration of respiratory syncytial virus immune globulin to high-risk infants and young children. The respiratory syncytial virus immune globulin study group. N. Engl. J. Med. 329 (1993), 1524–1530.
    • (1993) N. Engl. J. Med. , vol.329 , pp. 1524-1530
    • Groothuis, J.R.1    Simoes, E.A.2    Levin, M.J.3    Hall, C.B.4    Long, C.E.5    Rodriguez, W.J.6    Arrobio, J.7    Meissner, H.C.8    Fulton, D.R.9    Welliver, R.C.10
  • 47
    • 36849054036 scopus 로고    scopus 로고
    • Amino acid domains 280–297 of VP6 and 531–554 of VP4 are implicated in heat shock cognate protein hsc70-mediated rotavirus infection
    • Gualtero, D.F., Guzmán, F., Acosta, O., Guerrero, C.A., Amino acid domains 280–297 of VP6 and 531–554 of VP4 are implicated in heat shock cognate protein hsc70-mediated rotavirus infection. Arch. Virol. 152 (2007), 2183–2196.
    • (2007) Arch. Virol. , vol.152 , pp. 2183-2196
    • Gualtero, D.F.1    Guzmán, F.2    Acosta, O.3    Guerrero, C.A.4
  • 49
    • 0035927982 scopus 로고    scopus 로고
    • Respiratory syncytial virus and parainfluenza virus
    • Hall, C.B., Respiratory syncytial virus and parainfluenza virus. N. Engl. J. Med. 344 (2001), 1917–1928.
    • (2001) N. Engl. J. Med. , vol.344 , pp. 1917-1928
    • Hall, C.B.1
  • 52
    • 0032538278 scopus 로고    scopus 로고
    • Nef harbors a major determinant of pathogenicity for an AIDS-like disease induced by HIV-1 in transgenic mice
    • Hanna, Z., Kay, D.G., Rebai, N., Guimond, A., Jothy, S., Jolicoeur, P., Nef harbors a major determinant of pathogenicity for an AIDS-like disease induced by HIV-1 in transgenic mice. Cell 95 (1998), 163–175.
    • (1998) Cell , vol.95 , pp. 163-175
    • Hanna, Z.1    Kay, D.G.2    Rebai, N.3    Guimond, A.4    Jothy, S.5    Jolicoeur, P.6
  • 53
    • 35348819390 scopus 로고    scopus 로고
    • Properties, production, and applications of camelid single-domain antibody fragments
    • Harmsen, M.M., De Haard, H.J., Properties, production, and applications of camelid single-domain antibody fragments. Appl. Microbiol. Biotechnol. 77 (2007), 13–22.
    • (2007) Appl. Microbiol. Biotechnol. , vol.77 , pp. 13-22
    • Harmsen, M.M.1    De Haard, H.J.2
  • 54
    • 0034524838 scopus 로고    scopus 로고
    • Llama heavy-chain V regions consist of at least four distinct subfamilies revealing novel sequence features
    • Harmsen, M.M., Ruuls, R.C., Nijman, I.J., Niewold, T.A., Frenken, L.G., de Geus, B., Llama heavy-chain V regions consist of at least four distinct subfamilies revealing novel sequence features. Mol. Immunol. 37 (2000), 579–590.
    • (2000) Mol. Immunol. , vol.37 , pp. 579-590
    • Harmsen, M.M.1    Ruuls, R.C.2    Nijman, I.J.3    Niewold, T.A.4    Frenken, L.G.5    de Geus, B.6
  • 55
    • 24144458917 scopus 로고    scopus 로고
    • Prolonged in vivo residence times of llama single-domain antibody fragments in pigs by binding to porcine immunoglobulins
    • Harmsen, M.M., Van Solt, C.B., Fijten, H.P.D., Van Setten, M.C., Prolonged in vivo residence times of llama single-domain antibody fragments in pigs by binding to porcine immunoglobulins. Vaccine 23 (2005), 4926–4934.
    • (2005) Vaccine , vol.23 , pp. 4926-4934
    • Harmsen, M.M.1    Van Solt, C.B.2    Fijten, H.P.D.3    Van Setten, M.C.4
  • 58
    • 51649091611 scopus 로고    scopus 로고
    • Passive immunization of pigs with bispecific llama single-domain antibody fragments against foot-and-mouth disease and porcine immunoglobulin
    • Harmsen, M.M., Fijten, H.P.D., Dekker, A., Eblé, P.L., Passive immunization of pigs with bispecific llama single-domain antibody fragments against foot-and-mouth disease and porcine immunoglobulin. Vet. Microbiol. 132 (2008), 56–64.
    • (2008) Vet. Microbiol. , vol.132 , pp. 56-64
    • Harmsen, M.M.1    Fijten, H.P.D.2    Dekker, A.3    Eblé, P.L.4
  • 59
    • 70349680965 scopus 로고    scopus 로고
    • Enhancement of toxin- and virus-neutralizing capacity of single-domain antibody fragments by N-glycosylation
    • Harmsen, M.M., van Solt, C.B., Fijten, H.P.D., Enhancement of toxin- and virus-neutralizing capacity of single-domain antibody fragments by N-glycosylation. Appl. Microbiol. Biotechnol. 84 (2009), 1087–1094.
    • (2009) Appl. Microbiol. Biotechnol. , vol.84 , pp. 1087-1094
    • Harmsen, M.M.1    van Solt, C.B.2    Fijten, H.P.D.3
  • 60
    • 61349157275 scopus 로고    scopus 로고
    • Passive immunization with llama single-domain antibody fragments reduces foot-and-mouth disease transmission between pigs
    • Harmsen, M.M., Fijten, H.P.D., Engel, B., Dekker, A., Eblé, P.L., Passive immunization with llama single-domain antibody fragments reduces foot-and-mouth disease transmission between pigs. Vaccine 27 (2009), 1904–1911.
    • (2009) Vaccine , vol.27 , pp. 1904-1911
    • Harmsen, M.M.1    Fijten, H.P.D.2    Engel, B.3    Dekker, A.4    Eblé, P.L.5
  • 62
    • 0018760287 scopus 로고
    • Respiratory-syncytial-virus infections, reinfections and immunity. A prospective, longitudinal study in young children
    • Henderson, F.W., Collier, A.M., Clyde, W.A. Jr., Denny, F.W., Respiratory-syncytial-virus infections, reinfections and immunity. A prospective, longitudinal study in young children. N. Engl. J. Med 300 (1979), 530–534.
    • (1979) N. Engl. J. Med , vol.300 , pp. 530-534
    • Henderson, F.W.1    Collier, A.M.2    Clyde, W.A.3    Denny, F.W.4
  • 63
    • 0142227000 scopus 로고    scopus 로고
    • Critical overview and outlook: pathogenesis, prevention, and treatment of hepatitis and hepatocarcinoma caused by hepatitis B virus
    • Hilleman, M.R., Critical overview and outlook: pathogenesis, prevention, and treatment of hepatitis and hepatocarcinoma caused by hepatitis B virus. Vaccine 21 (2003), 4626–4649.
    • (2003) Vaccine , vol.21 , pp. 4626-4649
    • Hilleman, M.R.1
  • 66
    • 27144432842 scopus 로고    scopus 로고
    • Engineered antibody fragments and the rise of single domains
    • Holliger, P., Hudson, P.J., Engineered antibody fragments and the rise of single domains. Nat. Biotechnol. 23 (2005), 1126–1136.
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1126-1136
    • Holliger, P.1    Hudson, P.J.2
  • 72
    • 33846467193 scopus 로고    scopus 로고
    • Intracellular transport of hepatitis B virus
    • Kann, M., Schmitz, A., Rabe, B., Intracellular transport of hepatitis B virus. World J. Gastroenterol. 13 (2007), 39–47.
    • (2007) World J. Gastroenterol. , vol.13 , pp. 39-47
    • Kann, M.1    Schmitz, A.2    Rabe, B.3
  • 74
    • 59949088708 scopus 로고    scopus 로고
    • Selection and characterization of KDEL-specific VHH antibody fragments and their application in the study of ER resident protein expression
    • Klooster, R., Eman, M.R., le Duc, Q., Verheesen, P., Verrips, C.T., Roovers, R.C., Post, J.A., Selection and characterization of KDEL-specific VHH antibody fragments and their application in the study of ER resident protein expression. J. Immunol. Methods 342 (2009), 1–12.
    • (2009) J. Immunol. Methods , vol.342 , pp. 1-12
    • Klooster, R.1    Eman, M.R.2    le Duc, Q.3    Verheesen, P.4    Verrips, C.T.5    Roovers, R.C.6    Post, J.A.7
  • 77
    • 78149343713 scopus 로고    scopus 로고
    • Nanobodies-from llamas to therapeutic proteins
    • Kolkman, J.A., Law, D.A., Nanobodies-from llamas to therapeutic proteins. Drug Discov. Today: Technol. 7 (2010), e139–e146.
    • (2010) Drug Discov. Today: Technol. , vol.7 , pp. e139-e146
    • Kolkman, J.A.1    Law, D.A.2
  • 81
    • 32044449655 scopus 로고    scopus 로고
    • Worldwide epidemiology of HBV infection, disease burden, and vaccine prevention
    • Lavanchy, D., Worldwide epidemiology of HBV infection, disease burden, and vaccine prevention. J. Clin. Virol 34:Suppl. 1 (2005), S1–S3.
    • (2005) J. Clin. Virol , vol.34 , pp. S1-S3
    • Lavanchy, D.1
  • 82
    • 58949093626 scopus 로고    scopus 로고
    • Chronic viral hepatitis as a public health issue in the world
    • Lavanchy, D., Chronic viral hepatitis as a public health issue in the world. Best. Pract. Res. Clin. Gastroenterol. 22 (2008), 991–1008.
    • (2008) Best. Pract. Res. Clin. Gastroenterol. , vol.22 , pp. 991-1008
    • Lavanchy, D.1
  • 85
    • 33750357009 scopus 로고    scopus 로고
    • ES1, a new lung carcinoma antibody – an immunohistochemical study
    • Mai, K.T., Perkins, D.G., Zhang, J., Mackenzie, C.R., ES1, a new lung carcinoma antibody – an immunohistochemical study. Histopathology 49 (2006), 515–522.
    • (2006) Histopathology , vol.49 , pp. 515-522
    • Mai, K.T.1    Perkins, D.G.2    Zhang, J.3    Mackenzie, C.R.4
  • 86
    • 0024518918 scopus 로고
    • The HIV-1 rev trans-activator acts through a structured target sequence to activate nuclear export of unspliced viral mRNA
    • Malim, M.H., Hauber, J., Le, S.Y., Maizel, J.V., Cullen, B.R., The HIV-1 rev trans-activator acts through a structured target sequence to activate nuclear export of unspliced viral mRNA. Nature 338 (1989), 254–257.
    • (1989) Nature , vol.338 , pp. 254-257
    • Malim, M.H.1    Hauber, J.2    Le, S.Y.3    Maizel, J.V.4    Cullen, B.R.5
  • 88
    • 0032871808 scopus 로고    scopus 로고
    • Applications of phage resistance in lactic acid bacteria
    • Moineau, S., Applications of phage resistance in lactic acid bacteria. Antonie Van Leeuwenhoek 76 (1999), 377–382.
    • (1999) Antonie Van Leeuwenhoek , vol.76 , pp. 377-382
    • Moineau, S.1
  • 91
    • 35348965131 scopus 로고    scopus 로고
    • Use of neutralizing murine monoclonal antibodies to rabies glycoprotein in passive immunotherapy against rabies
    • Muhamuda, K., Madhusudana, S.N., Ravi, V., Use of neutralizing murine monoclonal antibodies to rabies glycoprotein in passive immunotherapy against rabies. Hum. Vaccine 3 (2007), 192–195.
    • (2007) Hum. Vaccine , vol.3 , pp. 192-195
    • Muhamuda, K.1    Madhusudana, S.N.2    Ravi, V.3
  • 93
    • 0028168145 scopus 로고
    • Sequence and structure of VH domain from naturally occurring camel heavy chain immunoglobulins lacking light chains
    • Muyldermans, S., Atarhouch, T., Saldanha, J., Barbosa, J.A., Hamers, R., Sequence and structure of VH domain from naturally occurring camel heavy chain immunoglobulins lacking light chains. Protein Eng. 7 (1994), 1129–1135.
    • (1994) Protein Eng. , vol.7 , pp. 1129-1135
    • Muyldermans, S.1    Atarhouch, T.2    Saldanha, J.3    Barbosa, J.A.4    Hamers, R.5
  • 94
    • 0035312546 scopus 로고    scopus 로고
    • Recognition of antigens by single-domain antibody fragments: the superfluous luxury of paired domains
    • Muyldermans, S., Cambillau, C., Wyns, L., Recognition of antigens by single-domain antibody fragments: the superfluous luxury of paired domains. Trends Biochem. Sci. 26 (2001), 230–235.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 230-235
    • Muyldermans, S.1    Cambillau, C.2    Wyns, L.3
  • 96
    • 0031260540 scopus 로고    scopus 로고
    • The importin-beta family member Crm1p bridges the interaction between Rev and the nuclear pore complex during nuclear export
    • Neville, M., Stutz, F., Lee, L., Davis, L.I., Rosbash, M., The importin-beta family member Crm1p bridges the interaction between Rev and the nuclear pore complex during nuclear export. Curr. Biol. 7 (1997), 767–775.
    • (1997) Curr. Biol. , vol.7 , pp. 767-775
    • Neville, M.1    Stutz, F.2    Lee, L.3    Davis, L.I.4    Rosbash, M.5
  • 97
    • 0345425685 scopus 로고    scopus 로고
    • Loss of splice consensus signal is responsible for the removal of the entire C(H)1 domain of the functional camel IGG2A heavy-chain antibodies
    • Nguyen, V.K., Hamers, R., Wyns, L., Muyldermans, S., Loss of splice consensus signal is responsible for the removal of the entire C(H)1 domain of the functional camel IGG2A heavy-chain antibodies. Mol. Immunol. 36 (1999), 515–524.
    • (1999) Mol. Immunol. , vol.36 , pp. 515-524
    • Nguyen, V.K.1    Hamers, R.2    Wyns, L.3    Muyldermans, S.4
  • 98
    • 0034161488 scopus 로고    scopus 로고
    • Camel heavy-chain antibodies: diverse germline V(H)H and specific mechanisms enlarge the antigen-binding repertoire
    • Nguyen, V.K., Hamers, R., Wyns, L., Muyldermans, S., Camel heavy-chain antibodies: diverse germline V(H)H and specific mechanisms enlarge the antigen-binding repertoire. EMBO J. 19 (2000), 921–930.
    • (2000) EMBO J. , vol.19 , pp. 921-930
    • Nguyen, V.K.1    Hamers, R.2    Wyns, L.3    Muyldermans, S.4
  • 99
    • 0034830063 scopus 로고    scopus 로고
    • Isolation of the new antigen receptor from wobbegong sharks, and use as a scaffold for the display of protein loop libraries
    • Nuttall, S.D., Krishnan, U.V., Hattarki, M., De Gori, R., Irving, R.A., Hudson, P.J., Isolation of the new antigen receptor from wobbegong sharks, and use as a scaffold for the display of protein loop libraries. Mol. Immunol. 38 (2001), 313–326.
    • (2001) Mol. Immunol. , vol.38 , pp. 313-326
    • Nuttall, S.D.1    Krishnan, U.V.2    Hattarki, M.3    De Gori, R.4    Irving, R.A.5    Hudson, P.J.6
  • 101
    • 0033588002 scopus 로고    scopus 로고
    • Search for cross-species transmission of porcine endogenous retrovirus in patients treated with living pig tissue. The XEN 111 Study Group
    • Paradis, K., Langford, G., Long, Z., Heneine, W., Sandstrom, P., Switzer, W.M., Chapman, L.E., Lockey, C., Onions, D., Otto, E., Search for cross-species transmission of porcine endogenous retrovirus in patients treated with living pig tissue. The XEN 111 Study Group. Science 285 (1999), 1236–1241.
    • (1999) Science , vol.285 , pp. 1236-1241
    • Paradis, K.1    Langford, G.2    Long, Z.3    Heneine, W.4    Sandstrom, P.5    Switzer, W.M.6    Chapman, L.E.7    Lockey, C.8    Onions, D.9    Otto, E.10
  • 103
    • 0031054438 scopus 로고    scopus 로고
    • Infection of human cells by an endogenous retrovirus of pigs
    • Patience, C., Takeuchi, Y., Weiss, R.A., Infection of human cells by an endogenous retrovirus of pigs. Nat. Med. 3 (1997), 282–286.
    • (1997) Nat. Med. , vol.3 , pp. 282-286
    • Patience, C.1    Takeuchi, Y.2    Weiss, R.A.3
  • 106
    • 0347991897 scopus 로고    scopus 로고
    • Ecologic and geographic distribution of filovirus disease
    • Peterson, A.T., Bauer, J.T., Mills, J.N., Ecologic and geographic distribution of filovirus disease. Emerging Infect. Dis. 10 (2004), 40–47.
    • (2004) Emerging Infect. Dis. , vol.10 , pp. 40-47
    • Peterson, A.T.1    Bauer, J.T.2    Mills, J.N.3
  • 108
    • 0036511140 scopus 로고    scopus 로고
    • Knocking out xenograft rejection
    • Platt, J.L., Knocking out xenograft rejection. Nat. Biotechnol. 20 (2002), 231–232.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 231-232
    • Platt, J.L.1
  • 110
    • 0022359386 scopus 로고
    • Immunoprophylaxis and immunotherapy of respiratory syncytial virus infection in the cotton rat
    • Prince, G.A., Hemming, V.G., Horswood, R.L., Chanock, R.M., Immunoprophylaxis and immunotherapy of respiratory syncytial virus infection in the cotton rat. Virus Res. 3 (1985), 193–206.
    • (1985) Virus Res. , vol.3 , pp. 193-206
    • Prince, G.A.1    Hemming, V.G.2    Horswood, R.L.3    Chanock, R.M.4
  • 111
    • 0042692926 scopus 로고    scopus 로고
    • Nuclear import of hepatitis B virus capsids and release of the viral genome
    • Rabe, B., Vlachou, A., Panté, N., Helenius, A., Kann, M., Nuclear import of hepatitis B virus capsids and release of the viral genome. Proc. Natl. Acad. Sci. USA 100 (2003), 9849–9854.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 9849-9854
    • Rabe, B.1    Vlachou, A.2    Panté, N.3    Helenius, A.4    Kann, M.5
  • 112
    • 0028291731 scopus 로고
    • Recognition properties of a panel of human recombinant Fab fragments to the CD4 binding site of gp120 that show differing abilities to neutralize human immunodeficiency virus type 1
    • Roben, P., Moore, J.P., Thali, M., Sodroski, J., Barbas, C.F. 3rd, Burton, D.R., Recognition properties of a panel of human recombinant Fab fragments to the CD4 binding site of gp120 that show differing abilities to neutralize human immunodeficiency virus type 1. J. Virol. 68 (1994), 4821–4828.
    • (1994) J. Virol. , vol.68 , pp. 4821-4828
    • Roben, P.1    Moore, J.P.2    Thali, M.3    Sodroski, J.4    Barbas, C.F.5    Burton, D.R.6
  • 115
    • 0036637385 scopus 로고    scopus 로고
    • The mannose-dependent epitope for neutralizing antibody 2G12 on human immunodeficiency virus type 1 glycoprotein gp120
    • Sanders, R.W., Venturi, M., Schiffner, L., Kalyanaraman, R., Katinger, H., Lloyd, K.O., Kwong, P.D., Moore, J.P., The mannose-dependent epitope for neutralizing antibody 2G12 on human immunodeficiency virus type 1 glycoprotein gp120. J. Virol. 76 (2002), 7293–7305.
    • (2002) J. Virol. , vol.76 , pp. 7293-7305
    • Sanders, R.W.1    Venturi, M.2    Schiffner, L.3    Kalyanaraman, R.4    Katinger, H.5    Lloyd, K.O.6    Kwong, P.D.7    Moore, J.P.8
  • 116
    • 0035155632 scopus 로고    scopus 로고
    • Randomized, placebo-controlled, clinical trial of hyperimmunized chicken egg yolk immunoglobulin in children with rotavirus diarrhea
    • Sarker, S.A., Casswall, T.H., Juneja, L.R., Hoq, E., Hossain, I., Fuchs, G.J., Hammarström, L., Randomized, placebo-controlled, clinical trial of hyperimmunized chicken egg yolk immunoglobulin in children with rotavirus diarrhea. J. Pediatr. Gastroenterol. Nutr. 32 (2001), 19–25.
    • (2001) J. Pediatr. Gastroenterol. Nutr. , vol.32 , pp. 19-25
    • Sarker, S.A.1    Casswall, T.H.2    Juneja, L.R.3    Hoq, E.4    Hossain, I.5    Fuchs, G.J.6    Hammarström, L.7
  • 117
    • 0033829661 scopus 로고    scopus 로고
    • Antibodies for the prevention and treatment of viral diseases
    • Sawyer, L.A., Antibodies for the prevention and treatment of viral diseases. Antiviral Res. 47 (2000), 57–77.
    • (2000) Antiviral Res. , vol.47 , pp. 57-77
    • Sawyer, L.A.1
  • 119
    • 58949094406 scopus 로고    scopus 로고
    • Llama-derived single-domain intrabodies inhibit secretion of hepatitis B virions in mice
    • Serruys, B., Van Houtte, F., Verbrugghe, P., Leroux-Roels, G., Vanlandschoot, P., Llama-derived single-domain intrabodies inhibit secretion of hepatitis B virions in mice. Hepatology 49 (2009), 39–49.
    • (2009) Hepatology , vol.49 , pp. 39-49
    • Serruys, B.1    Van Houtte, F.2    Verbrugghe, P.3    Leroux-Roels, G.4    Vanlandschoot, P.5
  • 120
    • 38449097605 scopus 로고    scopus 로고
    • Rapid assembly of sensitive antigen-capture assays for Marburg virus, using in vitro selection of llama single-domain antibodies, at biosafety level 4
    • Sherwood, L.J., Osborn, L.E., Carrion, R. Jr., Patterson, J.L., Hayhurst, A., Rapid assembly of sensitive antigen-capture assays for Marburg virus, using in vitro selection of llama single-domain antibodies, at biosafety level 4. J. Infect. Dis. 196:Suppl. 2 (2007), S213–S219.
    • (2007) J. Infect. Dis. , vol.196 , pp. S213-S219
    • Sherwood, L.J.1    Osborn, L.E.2    Carrion, R.3    Patterson, J.L.4    Hayhurst, A.5
  • 121
    • 0030378226 scopus 로고    scopus 로고
    • Respiratory syncytial virus-enriched globulin for the prevention of acute otitis media in high risk children
    • Simoes, E.A., Groothuis, J.R., Tristram, D.A., Allessi, K., Lehr, M.V., Siber, G.R., Welliver, R.C., Respiratory syncytial virus-enriched globulin for the prevention of acute otitis media in high risk children. J. Pediatr. 129 (1996), 214–219.
    • (1996) J. Pediatr. , vol.129 , pp. 214-219
    • Simoes, E.A.1    Groothuis, J.R.2    Tristram, D.A.3    Allessi, K.4    Lehr, M.V.5    Siber, G.R.6    Welliver, R.C.7
  • 122
    • 0035811873 scopus 로고    scopus 로고
    • Productive infection of human primary cells and cell lines with porcine endogenous retroviruses
    • Specke, V., Rubant, S., Denner, J., Productive infection of human primary cells and cell lines with porcine endogenous retroviruses. Virology 285 (2001), 177–180.
    • (2001) Virology , vol.285 , pp. 177-180
    • Specke, V.1    Rubant, S.2    Denner, J.3
  • 123
    • 30044442097 scopus 로고    scopus 로고
    • Lactococcal bacteriophage p2 receptor-binding protein structure suggests a common ancestor gene with bacterial and mammalian viruses
    • Spinelli, S., Desmyter, A., Verrips, C.T., de Haard, H.J.W., Moineau, S., Cambillau, C., Lactococcal bacteriophage p2 receptor-binding protein structure suggests a common ancestor gene with bacterial and mammalian viruses. Nat. Struct. Mol. Biol. 13 (2006), 85–89.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 85-89
    • Spinelli, S.1    Desmyter, A.2    Verrips, C.T.3    de Haard, H.J.W.4    Moineau, S.5    Cambillau, C.6
  • 124
    • 33947306907 scopus 로고    scopus 로고
    • Isolation, characterization and pentamerization of alpha-cobrotoxin specific single-domain antibodies from a naïve phage display library: preliminary findings for antivenom development
    • Stewart, C.S., MacKenzie, C.R., Hall, J.C., Isolation, characterization and pentamerization of alpha-cobrotoxin specific single-domain antibodies from a naïve phage display library: preliminary findings for antivenom development. Toxicon 49 (2007), 699–709.
    • (2007) Toxicon , vol.49 , pp. 699-709
    • Stewart, C.S.1    MacKenzie, C.R.2    Hall, J.C.3
  • 127
  • 131
    • 79954580247 scopus 로고    scopus 로고
    • A simple quantitative affinity capturing assay of poliovirus antigens and subviral particles by single-domain antibodies using magnetic beads
    • Thys, B., Saerens, D., Schotte, L., De Bleeser, G., Muyldermans, S., Hassanzadeh-Ghassabeh, G., Rombaut, B., A simple quantitative affinity capturing assay of poliovirus antigens and subviral particles by single-domain antibodies using magnetic beads. J. Virol. Methods 173 (2011), 300–305.
    • (2011) J. Virol. Methods , vol.173 , pp. 300-305
    • Thys, B.1    Saerens, D.2    Schotte, L.3    De Bleeser, G.4    Muyldermans, S.5    Hassanzadeh-Ghassabeh, G.6    Rombaut, B.7
  • 133
    • 53349171633 scopus 로고    scopus 로고
    • Improved tumor targeting of anti-epidermal growth factor receptor Nanobodies through albumin binding: taking advantage of modular Nanobody technology
    • Tijink, B.M., Laeremans, T., Budde, M., Stigter-van Walsum, M., Dreier, T., de Haard, H.J., Leemans, C.R., van Dongen, G.A.M.S., Improved tumor targeting of anti-epidermal growth factor receptor Nanobodies through albumin binding: taking advantage of modular Nanobody technology. Mol. Cancer Ther. 7 (2008), 2288–2297.
    • (2008) Mol. Cancer Ther. , vol.7 , pp. 2288-2297
    • Tijink, B.M.1    Laeremans, T.2    Budde, M.3    Stigter-van Walsum, M.4    Dreier, T.5    de Haard, H.J.6    Leemans, C.R.7    van Dongen, G.A.M.S.8
  • 135
    • 0031855323 scopus 로고    scopus 로고
    • Camel single-domain antibody inhibits enzyme by mimicking carbohydrate substrate
    • Transue, T.R., De Genst, E., Ghahroudi, M.A., Wyns, L., Muyldermans, S., Camel single-domain antibody inhibits enzyme by mimicking carbohydrate substrate. Proteins 32 (1998), 515–522.
    • (1998) Proteins , vol.32 , pp. 515-522
    • Transue, T.R.1    De Genst, E.2    Ghahroudi, M.A.3    Wyns, L.4    Muyldermans, S.5
  • 137
  • 139
    • 77954356408 scopus 로고    scopus 로고
    • An intrabody based on a llama single-domain antibody targeting the N-terminal alpha-helical multimerization domain of HIV-1 rev prevents viral production
    • Vercruysse, T., Pardon, E., Vanstreels, E., Steyaert, J., Daelemans, D., An intrabody based on a llama single-domain antibody targeting the N-terminal alpha-helical multimerization domain of HIV-1 rev prevents viral production. J. Biol. Chem. 285 (2010), 21768–21780.
    • (2010) J. Biol. Chem. , vol.285 , pp. 21768-21780
    • Vercruysse, T.1    Pardon, E.2    Vanstreels, E.3    Steyaert, J.4    Daelemans, D.5
  • 142
    • 59149104037 scopus 로고    scopus 로고
    • General strategy to humanize a camelid single-domain antibody and identification of a universal humanized nanobody scaffold
    • Vincke, C., Loris, R., Saerens, D., Martinez-Rodriguez, S., Muyldermans, S., Conrath, K., General strategy to humanize a camelid single-domain antibody and identification of a universal humanized nanobody scaffold. J. Biol. Chem. 284 (2009), 3273–3284.
    • (2009) J. Biol. Chem. , vol.284 , pp. 3273-3284
    • Vincke, C.1    Loris, R.2    Saerens, D.3    Martinez-Rodriguez, S.4    Muyldermans, S.5    Conrath, K.6
  • 143
    • 0031267747 scopus 로고    scopus 로고
    • Comparison of llama VH sequences from conventional and heavy chain antibodies
    • Vu, K.B., Ghahroudi, M.A., Wyns, L., Muyldermans, S., Comparison of llama VH sequences from conventional and heavy chain antibodies. Mol. Immunol. 34 (1997), 1121–1131.
    • (1997) Mol. Immunol. , vol.34 , pp. 1121-1131
    • Vu, K.B.1    Ghahroudi, M.A.2    Wyns, L.3    Muyldermans, S.4
  • 144
    • 0021363841 scopus 로고
    • Protection from respiratory syncytial virus infection in cotton rats by passive transfer of monoclonal antibodies
    • Walsh, E.E., Schlesinger, J.J., Brandriss, M.W., Protection from respiratory syncytial virus infection in cotton rats by passive transfer of monoclonal antibodies. Infect. Immun. 43 (1984), 756–758.
    • (1984) Infect. Immun. , vol.43 , pp. 756-758
    • Walsh, E.E.1    Schlesinger, J.J.2    Brandriss, M.W.3
  • 145
    • 63849116536 scopus 로고    scopus 로고
    • Mechanisms of protection against rotavirus infection and disease
    • Ward, R., Mechanisms of protection against rotavirus infection and disease. Pediatr. Infect. Dis. J. 28 (2009), S57–59.
    • (2009) Pediatr. Infect. Dis. J. , vol.28 , pp. S57-59
    • Ward, R.1
  • 146
    • 77952199776 scopus 로고    scopus 로고
    • Challenges faced by the global polio eradication initiative
    • Wassilak, S., Orenstein, W., Challenges faced by the global polio eradication initiative. Expert. Rev. Vaccines 9 (2010), 447–449.
    • (2010) Expert. Rev. Vaccines , vol.9 , pp. 447-449
    • Wassilak, S.1    Orenstein, W.2
  • 148
    • 0032841561 scopus 로고    scopus 로고
    • The structure of the llama heavy chain constant genes reveals a mechanism for heavy-chain antibody formation
    • Woolven, B.P., Frenken, L.G., van der Logt, P., Nicholls, P.J., The structure of the llama heavy chain constant genes reveals a mechanism for heavy-chain antibody formation. Immunogenetics 50 (1999), 98–101.
    • (1999) Immunogenetics , vol.50 , pp. 98-101
    • Woolven, B.P.1    Frenken, L.G.2    van der Logt, P.3    Nicholls, P.J.4
  • 149
    • 38449102652 scopus 로고    scopus 로고
    • Immunoprophylaxis of RSV infection: advancing from RSV-IGIV to palivizumab and motavizumab
    • Wu, H., Pfarr, D.S., Losonsky, G.A., Kiener, P.A., Immunoprophylaxis of RSV infection: advancing from RSV-IGIV to palivizumab and motavizumab. Curr. Top. Microbiol. Immunol. 317 (2008), 103–123.
    • (2008) Curr. Top. Microbiol. Immunol. , vol.317 , pp. 103-123
    • Wu, H.1    Pfarr, D.S.2    Losonsky, G.A.3    Kiener, P.A.4
  • 150
    • 0032546844 scopus 로고    scopus 로고
    • The HIV-1 envelope glycoproteins: fusogens, antigens, and immunogens
    • Wyatt, R., Sodroski, J., The HIV-1 envelope glycoproteins: fusogens, antigens, and immunogens. Science 280 (1998), 1884–1888.
    • (1998) Science , vol.280 , pp. 1884-1888
    • Wyatt, R.1    Sodroski, J.2
  • 152
    • 0037108818 scopus 로고    scopus 로고
    • Hydrodynamic injection of viral DNA: a mouse model of acute hepatitis B virus infection
    • Yang, P.L., Althage, A., Chung, J., Chisari, F.V., Hydrodynamic injection of viral DNA: a mouse model of acute hepatitis B virus infection. Proc. Natl. Acad. Sci. USA 99 (2002), 13825–13830.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 13825-13830
    • Yang, P.L.1    Althage, A.2    Chung, J.3    Chisari, F.V.4
  • 153
    • 0344255688 scopus 로고    scopus 로고
    • Pentamerization of single-domain antibodies from phage libraries: a novel strategy for the rapid generation of high-avidity antibody reagents
    • Zhang, J., Tanha, J., Hirama, T., Khieu, N.H., To, R., Tong-Sevinc, H., Stone, E., Brisson, J.R., MacKenzie, C.R., Pentamerization of single-domain antibodies from phage libraries: a novel strategy for the rapid generation of high-avidity antibody reagents. J. Mol. Biol. 335 (2004), 49–56.
    • (2004) J. Mol. Biol. , vol.335 , pp. 49-56
    • Zhang, J.1    Tanha, J.2    Hirama, T.3    Khieu, N.H.4    To, R.5    Tong-Sevinc, H.6    Stone, E.7    Brisson, J.R.8    MacKenzie, C.R.9
  • 155
    • 78650807161 scopus 로고    scopus 로고
    • Hepatitis B virus resistance to antiviral drugs: where are we going?
    • Zoulim, F., Hepatitis B virus resistance to antiviral drugs: where are we going?. Liver. Int. 31:Suppl. 1 (2011), 111–116.
    • (2011) Liver. Int. , vol.31 , pp. 111-116
    • Zoulim, F.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.