메뉴 건너뛰기




Volumn 1, Issue 2, 2007, Pages 149-155

Honey and royal jelly, like human milk, abrogate lectin-dependent infection-preceding Pseudomonas aeruginosa adhesion

Author keywords

Anti adhesion; Bacterial lectins; Honey; Infection therapy; Pseudomonas aeruginosa; Royal jelly

Indexed keywords

ADHESIN; ADHESIN, PSEUDOMONAS; CONCANAVALIN A; FATTY ACID; LECTIN; PLANT LECTIN; ROYAL JELLY; ULEX EUROPAEUS LECTINS; UNCLASSIFIED DRUG;

EID: 34249938369     PISSN: 17517362     EISSN: 17517370     Source Type: Journal    
DOI: 10.1038/ismej.2007.20     Document Type: Article
Times cited : (43)

References (39)
  • 2
    • 1642568737 scopus 로고    scopus 로고
    • The MRJP/YELLOW protein family of Apis mellifera: Identification of new members in the EST library
    • Albert S, Klaudiny J. (2004). The MRJP/YELLOW protein family of Apis mellifera: identification of new members in the EST library. / Insect Physiol 50: 51-59.
    • (2004) Insect Physiol , vol.50 , pp. 51-59
    • Albert, S.1    Klaudiny, J.2
  • 3
    • 0036861597 scopus 로고    scopus 로고
    • The efficacy of honey in inhibiting strains of Pseudomonas aeruginosa from infected burns
    • Cooper RA, Halas E, Molan PC. (2002). The efficacy of honey in inhibiting strains of Pseudomonas aeruginosa from infected burns. J Burn Care Rehabil 23: 366-370.
    • (2002) J Burn Care Rehabil , vol.23 , pp. 366-370
    • Cooper, R.A.1    Halas, E.2    Molan, P.C.3
  • 4
    • 33745171425 scopus 로고    scopus 로고
    • The galactophilic lectin, LecA, contributes to biofilm development in Pseudomonas aeruginosa
    • Diggle SP, Stacey RE, Dodd C, Camara M, Williams P, Winzer K. (2006). The galactophilic lectin, LecA, contributes to biofilm development in Pseudomonas aeruginosa. Environ Microbiol 8: 1095-1104.
    • (2006) Environ Microbiol , vol.8 , pp. 1095-1104
    • Diggle, S.P.1    Stacey, R.E.2    Dodd, C.3    Camara, M.4    Williams, P.5    Winzer, K.6
  • 5
    • 33750454258 scopus 로고    scopus 로고
    • Evolution of the Yellow/Major Royal Jelly Protein family and the emergence of social behavior in honey bees
    • Drapeau MD, Albert S, Kucharski R, Prusko C, Maleszka R. (2006). Evolution of the Yellow/Major Royal Jelly Protein family and the emergence of social behavior in honey bees. Genome Res 16: 1385-1394.
    • (2006) Genome Res , vol.16 , pp. 1385-1394
    • Drapeau, M.D.1    Albert, S.2    Kucharski, R.3    Prusko, C.4    Maleszka, R.5
  • 6
    • 24044498346 scopus 로고    scopus 로고
    • The antibacterial activity of honey against coagulase-negative staphylococci
    • French VM, Cooper RA, Molan PC. (2005). The antibacterial activity of honey against coagulase-negative staphylococci. J Antimicrob Chemother 56: 228-231.
    • (2005) J Antimicrob Chemother , vol.56 , pp. 228-231
    • French, V.M.1    Cooper, R.A.2    Molan, P.C.3
  • 7
    • 0020014208 scopus 로고
    • Pseudomonas aeruginosa lectins
    • Gilboa-Garber N. (1982). Pseudomonas aeruginosa lectins. Methods Enzymol 83: 378-385.
    • (1982) Methods Enzymol , vol.83 , pp. 378-385
    • Gilboa-Garber, N.1
  • 8
    • 0029745141 scopus 로고    scopus 로고
    • Towards anti-Pseudomonas aeruginosa adhesion therapy
    • Gilboa-Garber N. (1996). Towards anti-Pseudomonas aeruginosa adhesion therapy. Adv Exp Med Biol 408: 39-50.
    • (1996) Adv Exp Med Biol , vol.408 , pp. 39-50
    • Gilboa-Garber, N.1
  • 9
    • 0003158439 scopus 로고    scopus 로고
    • Bacterial lectins: Properties, structure, effects, function and applications
    • Gabius H-J, Gabius S eds, Chapman & Hall: Weinheim, pp
    • Gilboa-Garber N, Avichezer D, Garber NC. (1997). Bacterial lectins: properties, structure, effects, function and applications. In: Gabius H-J, Gabius S (eds). Glycosciences: Status and Perspectives. Chapman & Hall: Weinheim, pp 369-398.
    • (1997) Glycosciences: Status and Perspectives , pp. 369-398
    • Gilboa-Garber, N.1    Avichezer, D.2    Garber, N.C.3
  • 11
    • 0034296913 scopus 로고    scopus 로고
    • Structural features of N-glycans linked to royal jelly glycoproteins: Structures of high-mannose type, hybrid type, and biantennary type glycans
    • Kimura Y, Miyagi C, Kimura M, Nitoda T, Kawai N, Sugimoto H. (2000). Structural features of N-glycans linked to royal jelly glycoproteins: structures of high-mannose type, hybrid type, and biantennary type glycans. Biosci Biotechnol Biochem 64: 2109-2120.
    • (2000) Biosci Biotechnol Biochem , vol.64 , pp. 2109-2120
    • Kimura, Y.1    Miyagi, C.2    Kimura, M.3    Nitoda, T.4    Kawai, N.5    Sugimoto, H.6
  • 12
    • 0025827987 scopus 로고
    • The primary structures of two types of the Ulex europeus seed lectin
    • Konami Y, Yamamoto K, Osawa T. (1991). The primary structures of two types of the Ulex europeus seed lectin. J Biochem (Tokyo) 109: 650-658.
    • (1991) J Biochem (Tokyo) , vol.109 , pp. 650-658
    • Konami, Y.1    Yamamoto, K.2    Osawa, T.3
  • 13
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 14
    • 0035720004 scopus 로고    scopus 로고
    • Interactions of Pseudomonas aeruginosa PA-II lectin with quail egg white glycoproteins
    • Lerrer B, Gilboa-Garber N. (2001). Interactions of Pseudomonas aeruginosa PA-II lectin with quail egg white glycoproteins. Can J Microbiol 47: 1095-1100.
    • (2001) Can J Microbiol , vol.47 , pp. 1095-1100
    • Lerrer, B.1    Gilboa-Garber, N.2
  • 15
    • 0141720786 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa lectin PA-IIL as a powerful probe for human and bovine milk analysis
    • Lesman-Movshovich E, Gilboa-Garber N. (2003). Pseudomonas aeruginosa lectin PA-IIL as a powerful probe for human and bovine milk analysis. J Dairy Sci 86: 2276-2282.
    • (2003) J Dairy Sci , vol.86 , pp. 2276-2282
    • Lesman-Movshovich, E.1    Gilboa-Garber, N.2
  • 16
    • 0038209572 scopus 로고    scopus 로고
    • Blocking of Pseudomonas aeruginosa lectins by human milk glycans
    • Lesman-Movshovich E, Lerrer B, Gilboa-Garber N. (2003). Blocking of Pseudomonas aeruginosa lectins by human milk glycans. Can J Microbiol 49: 230-235.
    • (2003) Can J Microbiol , vol.49 , pp. 230-235
    • Lesman-Movshovich, E.1    Lerrer, B.2    Gilboa-Garber, N.3
  • 17
    • 30144437355 scopus 로고    scopus 로고
    • The immunostimulatory effect of the recombinant apalbumin 1-major honeybee royal jelly protein-on TNFalpha release
    • Majtan J, Kovacova E, Bilikova K, Simuth J. (2006). The immunostimulatory effect of the recombinant apalbumin 1-major honeybee royal jelly protein-on TNFalpha release. Int Immunopharmacol 6: 269-278.
    • (2006) Int Immunopharmacol , vol.6 , pp. 269-278
    • Majtan, J.1    Kovacova, E.2    Bilikova, K.3    Simuth, J.4
  • 18
    • 0036895829 scopus 로고    scopus 로고
    • Structural basis for oligosaccharide-mediated adhesion of Pseudomonas aeruginosa in the lung of cystic fibrosis patients
    • Mitchell E, Houles C, Sudakevitz D, Wimmerova M, Gautier C, Perez S et al. (2002). Structural basis for oligosaccharide-mediated adhesion of Pseudomonas aeruginosa in the lung of cystic fibrosis patients. Nat Struct Biol 9: 918-921.
    • (2002) Nat Struct Biol , vol.9 , pp. 918-921
    • Mitchell, E.1    Houles, C.2    Sudakevitz, D.3    Wimmerova, M.4    Gautier, C.5    Perez, S.6
  • 19
    • 32944458742 scopus 로고    scopus 로고
    • The evidence supporting the use of honey as a wound dressing
    • Molan PC. (2006). The evidence supporting the use of honey as a wound dressing. Int J Low Extrem Wounds 5: 40-54.
    • (2006) Int J Low Extrem Wounds , vol.5 , pp. 40-54
    • Molan, P.C.1
  • 20
    • 0031934283 scopus 로고    scopus 로고
    • Concanavalin A distorts the beta-GlcNAc-(1→2)-Man linkage of beta-GlcNAc-(1→2)-alpha-Man- (1→3)-[beta-GlcNAc-(1→2)-alpha-Man-(1→6)]-Man upon binding
    • Moothoo DN, Naismith JH. (1998). Concanavalin A distorts the beta-GlcNAc-(1→2)-Man linkage of beta-GlcNAc-(1→2)-alpha-Man- (1→3)-[beta-GlcNAc-(1→2)-alpha-Man-(1→6)]-Man upon binding. Glycobiology 8: 173-181.
    • (1998) Glycobiology , vol.8 , pp. 173-181
    • Moothoo, D.N.1    Naismith, J.H.2
  • 21
    • 34249936903 scopus 로고    scopus 로고
    • Moritz RFA, Southwick EE. (1992). Bees as Superorganisms - An Evolutionary Reality. Springer Verlag: Berlin, Heidelberg.
    • Moritz RFA, Southwick EE. (1992). Bees as Superorganisms - An Evolutionary Reality. Springer Verlag: Berlin, Heidelberg.
  • 22
    • 18344392519 scopus 로고    scopus 로고
    • Human-milk glycans that inhibit pathogen binding protect breast-feeding infants against infectious diarrhea
    • Morrow AL, Ruiz-Palacios GM, Jiang X, Newburg DS. (2005). Human-milk glycans that inhibit pathogen binding protect breast-feeding infants against infectious diarrhea. J Nutr 135: 1304-1307.
    • (2005) J Nutr , vol.135 , pp. 1304-1307
    • Morrow, A.L.1    Ruiz-Palacios, G.M.2    Jiang, X.3    Newburg, D.S.4
  • 23
    • 23944482922 scopus 로고    scopus 로고
    • Human milk glycans protect infants against enteric pathogens
    • Newburg DS, Ruiz-Palacios GM, Morrow AL. (2005). Human milk glycans protect infants against enteric pathogens. Annu Rev Nutr 25: 37-58.
    • (2005) Annu Rev Nutr , vol.25 , pp. 37-58
    • Newburg, D.S.1    Ruiz-Palacios, G.M.2    Morrow, A.L.3
  • 24
    • 0021809838 scopus 로고
    • The contribution of exoproducts to virulence of Pseudomonas aeruginosa
    • Nicas TI, Iglewski BH. (1985). The contribution of exoproducts to virulence of Pseudomonas aeruginosa. Can J Microbiol 31: 387-392.
    • (1985) Can J Microbiol , vol.31 , pp. 387-392
    • Nicas, T.I.1    Iglewski, B.H.2
  • 25
    • 22544487502 scopus 로고    scopus 로고
    • Structural basis for the interaction between human milk oligosaccharides and the bacterial lectin PA-IIL of Pseudomonas aeruginosa
    • Perret S, Sabin C, Dumon C, Pokorna M, Gautier C, Galanina O et al. (2005). Structural basis for the interaction between human milk oligosaccharides and the bacterial lectin PA-IIL of Pseudomonas aeruginosa. Biochem J 389: 325-332.
    • (2005) Biochem J , vol.389 , pp. 325-332
    • Perret, S.1    Sabin, C.2    Dumon, C.3    Pokorna, M.4    Gautier, C.5    Galanina, O.6
  • 26
    • 0032869370 scopus 로고    scopus 로고
    • Determination of chemical composition of commercial honey by near-infrared spectroscopy
    • Qiu PY, Ding HB, Tang YK, Xu RJ. (1999). Determination of chemical composition of commercial honey by near-infrared spectroscopy. J Agric Food Chem 47: 2760-2765.
    • (1999) J Agric Food Chem , vol.47 , pp. 2760-2765
    • Qiu, P.Y.1    Ding, H.B.2    Tang, Y.K.3    Xu, R.J.4
  • 27
    • 34249939040 scopus 로고    scopus 로고
    • Ruiz-Palacios GM, Cervantes LE, Ramos P, Chavez-Munguia B, Newburg DS. (2003). Campylobacter jejuni binds intestinal H(O) antigen (Fuc alpha 1, 2Gal beta 1, 4GlcNAc), and fucosyloligosaccharides of
    • Ruiz-Palacios GM, Cervantes LE, Ramos P, Chavez-Munguia B, Newburg DS. (2003). Campylobacter jejuni binds intestinal H(O) antigen (Fuc alpha 1, 2Gal beta 1, 4GlcNAc), and fucosyloligosaccharides of
  • 28
    • 0013238319 scopus 로고    scopus 로고
    • human milk Inhibit its binding and infection, J Biol Chem 278: 14112-14120.
    • human milk Inhibit its binding and infection, J Biol Chem 278: 14112-14120.
  • 29
    • 0347355029 scopus 로고    scopus 로고
    • Characterization of royal jelly proteins in both Africanized and European honeybees (Apis mellifera) by two-dimensional gel electrophoresis
    • Sano O, Kunikata T, Kohno K, Iwaki K, Ikeda M, Kurimoto M. (2004), Characterization of royal jelly proteins in both Africanized and European honeybees (Apis mellifera) by two-dimensional gel electrophoresis, JAgric Food Chem 52: 15-20.
    • (2004) JAgric Food Chem , vol.52 , pp. 15-20
    • Sano, O.1    Kunikata, T.2    Kohno, K.3    Iwaki, K.4    Ikeda, M.5    Kurimoto, M.6
  • 30
    • 10944245809 scopus 로고    scopus 로고
    • Profiling the proteome complement of the secretion from hypopharyngeal gland of Africanized nurse-honeybees (Apis mellifera L.)
    • Santos KS, dos Santos LD, Mendes MA, de Souza BM, Malasplna O, Palma MS, (2005), Profiling the proteome complement of the secretion from hypopharyngeal gland of Africanized nurse-honeybees (Apis mellifera L.), Insect Biochem Mol Biol 35: 85-91.
    • (2005) Insect Biochem Mol Biol , vol.35 , pp. 85-91
    • Santos, K.S.1    dos Santos, L.D.2    Mendes, M.A.3    de Souza, B.M.4    Malasplna, O.5    Palma, M.S.6
  • 33
    • 33646103431 scopus 로고    scopus 로고
    • Carbohydrates as future anti-adhesion drugs for infectious diseases
    • Sharon N. (2006), Carbohydrates as future anti-adhesion drugs for infectious diseases, Biochim Biophys Acta 1780: 527-537.
    • (2006) Biochim Biophys Acta , vol.1780 , pp. 527-537
    • Sharon, N.1
  • 34
    • 11144356043 scopus 로고    scopus 로고
    • Immunochemical approach to detection of adulteration in honey: Physiologically active royal jelly protein stimulating TNF-alpha release is a regular component of honey
    • Simuth J, Bilikova K, Kovacova E, Kuzmova Z, Schroder W. (2004), Immunochemical approach to detection of adulteration in honey: physiologically active royal jelly protein stimulating TNF-alpha release is a regular component of honey, J Agric Food Chem 52: 2154-2158.
    • (2004) J Agric Food Chem , vol.52 , pp. 2154-2158
    • Simuth, J.1    Bilikova, K.2    Kovacova, E.3    Kuzmova, Z.4    Schroder, W.5
  • 35
    • 27744584964 scopus 로고    scopus 로고
    • Trace and mineral elements in royal jelly and homeostatic effects
    • Stocker A, Schramel F, Kettrup A, Bengsch E, (2005), Trace and mineral elements in royal jelly and homeostatic effects. J Trace Elem Med Biol 19: 183-189.
    • (2005) J Trace Elem Med Biol , vol.19 , pp. 183-189
    • Stocker, A.1    Schramel, F.2    Kettrup, A.3    Bengsch, E.4
  • 36
    • 0003120738 scopus 로고
    • Chemical composition of royal jelly
    • Takenaka T. (1982), Chemical composition of royal jelly. Honeybee Sci 3: 69-74.
    • (1982) Honeybee Sci , vol.3 , pp. 69-74
    • Takenaka, T.1
  • 37
    • 0035964991 scopus 로고    scopus 로고
    • Inhibitory activity of honey against foodborne pathogens as influenced by the presence of hydrogen peroxide and level of antioxidant power
    • Taormina PJ, Niemira BA, Beuchat LR. (2001). Inhibitory activity of honey against foodborne pathogens as influenced by the presence of hydrogen peroxide and level of antioxidant power. Int J Food Microbiol 69: 217-225.
    • (2001) Int J Food Microbiol , vol.69 , pp. 217-225
    • Taormina, P.J.1    Niemira, B.A.2    Beuchat, L.R.3
  • 38
    • 19044365015 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa lectin LecB is located in the outer membrane and is involved in biofilm formation
    • Tielker D, Hacker S, Loris R, Strathmann M, Wingender J, Wilhelm S et al. (2005). Pseudomonas aeruginosa lectin LecB is located in the outer membrane and is involved in biofilm formation, Microbiology 151: 1313-1323.
    • (2005) Microbiology , vol.151 , pp. 1313-1323
    • Tielker, D.1    Hacker, S.2    Loris, R.3    Strathmann, M.4    Wingender, J.5    Wilhelm, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.