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Volumn 91, Issue 3, 2017, Pages

Inclusion body fusion of human parainfluenza virus type 3 regulated by acetylated α-tubulin enhances viral replication

Author keywords

Acetylated tubulin; Human parainfluenza virus type 3; Inclusion bodies

Indexed keywords

ACYLTRANSFERASE; ALPHA TUBULIN; ALPHA TUBULIN ACETYLTRANSFERASE 1; GLYCINE DEHYDROGENASE (DECARBOXYLATING); GUANINE NUCLEOTIDE BINDING PROTEIN; HISTONE DEACETYLASE 6; SIRTUIN 2; UNCLASSIFIED DRUG; PROTEIN BINDING; TUBULIN; VIRAL PROTEIN; VIRUS RNA;

EID: 85010867700     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.01802-16     Document Type: Article
Times cited : (41)

References (32)
  • 1
    • 0000078350 scopus 로고    scopus 로고
    • Parainfluenza viruses
    • Knipe DM, Howley PM (ed), Lippincott-Raven Publications, Philadelphia, PA
    • Collins PL, Chanock RM, McIntosh K. 1996. Parainfluenza viruses, p 1205-1241. In Knipe DM, Howley PM (ed), Fields virology. Lippincott-Raven Publications, Philadelphia, PA.
    • (1996) Fields virology , pp. 1205-1241
    • Collins, P.L.1    Chanock, R.M.2    McIntosh, K.3
  • 2
    • 0031575842 scopus 로고    scopus 로고
    • A highly conserved region of the Sendai virus nucleocapsid protein contributes to the NP-NP binding domain
    • Myers TM, Pieters A, Moyer SA. 1997. A highly conserved region of the Sendai virus nucleocapsid protein contributes to the NP-NP binding domain. Virology 229:322-335. https://doi.org/10.1006/viro.1996.8429.
    • (1997) Virology , vol.229 , pp. 322-335
    • Myers, T.M.1    Pieters, A.2    Moyer, S.A.3
  • 3
    • 0036337962 scopus 로고    scopus 로고
    • Identification and characterization of a regulatory domain on the carboxyl terminus of the measles virus nucleocapsid protein
    • Zhang X, Glendening C, Linke H, Parks CL, Brooks C, Udem SA, Oglesbee M. 2002. Identification and characterization of a regulatory domain on the carboxyl terminus of the measles virus nucleocapsid protein. J Virol 76:8737-8746. https://doi.org/10.1128/JVI.76.17.8737-8746.2002.
    • (2002) J Virol , vol.76 , pp. 8737-8746
    • Zhang, X.1    Glendening, C.2    Linke, H.3    Parks, C.L.4    Brooks, C.5    Udem, S.A.6    Oglesbee, M.7
  • 4
    • 0028895953 scopus 로고
    • An N-terminal domain of the Sendai paramyxovirus P protein acts as a chaperone for the NP protein during the nascent chain assembly step of genome replication
    • Curran J, Marq JB, Kolakofsky D. 1995. An N-terminal domain of the Sendai paramyxovirus P protein acts as a chaperone for the NP protein during the nascent chain assembly step of genome replication. J Virol 69:849-855.
    • (1995) J Virol , vol.69 , pp. 849-855
    • Curran, J.1    Marq, J.B.2    Kolakofsky, D.3
  • 5
    • 0024453774 scopus 로고
    • Vesicular stomatitis virus RNA replication: a role for the NS protein
    • Howard M, Wertz G. 1989. Vesicular stomatitis virus RNA replication: a role for the NS protein. J Gen Virol 70:2683-2694. https://doi.org/10.1099/0022-1317-70-10-2683.
    • (1989) J Gen Virol , vol.70 , pp. 2683-2694
    • Howard, M.1    Wertz, G.2
  • 6
    • 37049018431 scopus 로고    scopus 로고
    • Interaction of vesicular stomatitis virus P and N proteins: identification of two overlapping domains at the N terminus of P that are involved in N0-P complex formation and encapsidation of viral genome RNA
    • Chen M, Ogino T, Banerjee AK. 2007. Interaction of vesicular stomatitis virus P and N proteins: identification of two overlapping domains at the N terminus of P that are involved in N0-P complex formation and encapsidation of viral genome RNA. J Virol 81:13478-13485. https://doi.org/10.1128/JVI.01244-07.
    • (2007) J Virol , vol.81 , pp. 13478-13485
    • Chen, M.1    Ogino, T.2    Banerjee, A.K.3
  • 7
    • 0342757599 scopus 로고    scopus 로고
    • Role of NH(2)-and COOH-terminal domains of the P protein of human parainfluenza virus type 3 in transcription and replication
    • De BP, Hoffman MA, Choudhary S, Huntley CC, Banerjee AK. 2000. Role of NH(2)-and COOH-terminal domains of the P protein of human parainfluenza virus type 3 in transcription and replication. J Virol 74: 5886-5895. https://doi.org/10.1128/JVI.74.13.5886-5895.2000.
    • (2000) J Virol , vol.74 , pp. 5886-5895
    • De, B.P.1    Hoffman, M.A.2    Choudhary, S.3    Huntley, C.C.4    Banerjee, A.K.5
  • 8
    • 0036441132 scopus 로고    scopus 로고
    • Characterization of the oligomerization domain of the phosphoprotein of human parainfluenza virus type 3
    • Choudhary SK, Malur AG, Huo Y, De BP, Banerjee AK. 2002. Characterization of the oligomerization domain of the phosphoprotein of human parainfluenza virus type 3. Virology 302:373-382. https://doi.org/10.1006/viro.2002.1668.
    • (2002) Virology , vol.302 , pp. 373-382
    • Choudhary, S.K.1    Malur, A.G.2    Huo, Y.3    De, B.P.4    Banerjee, A.K.5
  • 9
    • 34548238709 scopus 로고    scopus 로고
    • A guide to viral inclusions, membrane rearrangements, factories, and viroplasm produced during virus replication
    • Netherton C, Moffat K, Brooks E, Wileman T. 2007. A guide to viral inclusions, membrane rearrangements, factories, and viroplasm produced during virus replication. Adv Virus Res 70:101-182. https://doi.org/10.1016/S0065-3527(07)70004-0.
    • (2007) Adv Virus Res , vol.70 , pp. 101-182
    • Netherton, C.1    Moffat, K.2    Brooks, E.3    Wileman, T.4
  • 10
    • 0027257384 scopus 로고
    • Cytoplasmic inclusions of respiratory syncytial virus-infected cells: formation of inclusion bodies in transfected cells that coexpress the nucleoprotein, the phosphoprotein, and the 22K protein
    • Garcia J, Garcia-Barreno B, Vivo A, Melero JA. 1993. Cytoplasmic inclusions of respiratory syncytial virus-infected cells: formation of inclusion bodies in transfected cells that coexpress the nucleoprotein, the phosphoprotein, and the 22K protein. Virology 195:243-247. https://doi.org/10.1006/viro.1993.1366.
    • (1993) Virology , vol.195 , pp. 243-247
    • Garcia, J.1    Garcia-Barreno, B.2    Vivo, A.3    Melero, J.A.4
  • 11
    • 67749104678 scopus 로고    scopus 로고
    • Functional characterization of Negri bodies (NBs) in rabies virusinfected cells: evidence that NBs are sites of viral transcription and replication
    • Lahaye X, Vidy A, Pomier C, Obiang L, Harper F, Gaudin Y, Blondel D. 2009 Functional characterization of Negri bodies (NBs) in rabies virusinfected cells: evidence that NBs are sites of viral transcription and replication. J Virol 83:7948-7958. https://doi.org/10.1128/JVI.00554-09.
    • (2009) J Virol , vol.83 , pp. 7948-7958
    • Lahaye, X.1    Vidy, A.2    Pomier, C.3    Obiang, L.4    Harper, F.5    Gaudin, Y.6    Blondel, D.7
  • 12
    • 56349087485 scopus 로고    scopus 로고
    • Human metapneumovirus nucleoprotein and phosphoprotein interact and provide the minimal requirements for inclusion body formation
    • Derdowski A, Peters TR, Glover N, Qian R, Utley TJ, Burnett A, Williams JV, Spearman P, Crowe JE, Jr. 2008. Human metapneumovirus nucleoprotein and phosphoprotein interact and provide the minimal requirements for inclusion body formation. J Gen Virol 89:2698-2708. https://doi.org/10.1099/vir.0.2008/004051-0.
    • (2008) J Gen Virol , vol.89 , pp. 2698-2708
    • Derdowski, A.1    Peters, T.R.2    Glover, N.3    Qian, R.4    Utley, T.J.5    Burnett, A.6    Williams, J.V.7    Spearman, P.8    Crowe, J.E.9
  • 13
    • 84886263368 scopus 로고    scopus 로고
    • An amino acid of human parainfluenza virus type 3 nucleoprotein is critical for template function and cytoplasmic inclusion body formation
    • Zhang S, Chen L, Zhang G, Yan Q, Yang X, Ding B, Tang Q, Sun S, Hu Z, Chen M. 2013. An amino acid of human parainfluenza virus type 3 nucleoprotein is critical for template function and cytoplasmic inclusion body formation. J Virol 87:12457-12470. https://doi.org/10.1128/JVI.01565-13.
    • (2013) J Virol , vol.87 , pp. 12457-12470
    • Zhang, S.1    Chen, L.2    Zhang, G.3    Yan, Q.4    Yang, X.5    Ding, B.6    Tang, Q.7    Sun, S.8    Hu, Z.9    Chen, M.10
  • 15
    • 84864391552 scopus 로고    scopus 로고
    • Human respiratory syncytial virus nucleoprotein and inclusion bodies antagonize the innate immune response mediated by MDA5 and MAVS
    • Lifland AW, Jung J, Alonas E, Zurla C, Crowe JE, Jr, Santangelo PJ. 2012. Human respiratory syncytial virus nucleoprotein and inclusion bodies antagonize the innate immune response mediated by MDA5 and MAVS. J Virol 86:8245-8258. https://doi.org/10.1128/JVI.00215-12.
    • (2012) J Virol , vol.86 , pp. 8245-8258
    • Lifland, A.W.1    Jung, J.2    Alonas, E.3    Zurla, C.4    Crowe, J.E.5    Santangelo, P.J.6
  • 16
    • 0033989377 scopus 로고    scopus 로고
    • Profilin is required for optimal actin-dependent transcription of respiratory syncytial virus genome RNA
    • Burke E, Mahoney NM, Almo SC, Barik S. 2000. Profilin is required for optimal actin-dependent transcription of respiratory syncytial virus genome RNA. J Virol 74:669-675. https://doi.org/10.1128/JVI.74.2.669-675.2000.
    • (2000) J Virol , vol.74 , pp. 669-675
    • Burke, E.1    Mahoney, N.M.2    Almo, S.C.3    Barik, S.4
  • 17
    • 0017799006 scopus 로고
    • Structural polypeptides of measles virus
    • Tyrrell DL, Norrby E. 1978. Structural polypeptides of measles virus. J Gen Virol 39:219-229. https://doi.org/10.1099/0022-1317-39-2-219.
    • (1978) J Gen Virol , vol.39 , pp. 219-229
    • Tyrrell, D.L.1    Norrby, E.2
  • 18
    • 0022452231 scopus 로고
    • The acetylation of alpha-tubulin and its relationship to the assembly and disassembly of microtubules
    • Maruta H, Greer K, Rosenbaum JL. 1986. The acetylation of alpha-tubulin and its relationship to the assembly and disassembly of microtubules. J Cell Biol 103:571-579. https://doi.org/10.1083/jcb.103.2.571.
    • (1986) J Cell Biol , vol.103 , pp. 571-579
    • Maruta, H.1    Greer, K.2    Rosenbaum, J.L.3
  • 19
    • 84892547110 scopus 로고    scopus 로고
    • Effects of tubulin acetylation and tubulin acetyltransferase binding on microtubule structure
    • Howes SC, Alushin GM, Shida T, Nachury MV, Nogales E. 2014. Effects of tubulin acetylation and tubulin acetyltransferase binding on microtubule structure. Mol Biol Cell 25:257-266. https://doi.org/10.1091/mbc.E13-07-0387.
    • (2014) Mol Biol Cell , vol.25 , pp. 257-266
    • Howes, S.C.1    Alushin, G.M.2    Shida, T.3    Nachury, M.V.4    Nogales, E.5
  • 20
    • 84868146124 scopus 로고    scopus 로고
    • Luminal localization of alpha-tubulin K40 acetylation by cryo-EM analysis of fab-labeled microtubules
    • Soppina V, Herbstman JF, Skiniotis G, Verhey KJ. 2012. Luminal localization of alpha-tubulin K40 acetylation by cryo-EM analysis of fab-labeled microtubules. PLoS One 7:e48204. https://doi.org/10.1371/journal.pone.0048204.
    • (2012) PLoS One , vol.7
    • Soppina, V.1    Herbstman, J.F.2    Skiniotis, G.3    Verhey, K.J.4
  • 21
    • 84864746082 scopus 로고    scopus 로고
    • Tubulin acetylation alone does not affect kinesin-1 velocity and run length in vitro
    • Walter WJ, Beranek V, Fischermeier E, Diez S. 2012. Tubulin acetylation alone does not affect kinesin-1 velocity and run length in vitro. PLoS One 7:e42218. https://doi.org/10.1371/journal.pone.0042218.
    • (2012) PLoS One , vol.7
    • Walter, W.J.1    Beranek, V.2    Fischermeier, E.3    Diez, S.4
  • 23
    • 0037448422 scopus 로고    scopus 로고
    • Involvement of acetylated tubulin in the regulation of Na+, K+-ATPase activity in cultured astrocytes
    • Casale CH, Previtali G, Barra HS. 2003. Involvement of acetylated tubulin in the regulation of Na+, K+-ATPase activity in cultured astrocytes. FEBS Lett 534:115-118. https://doi.org/10.1016/S0014-5793(02)03802-4.
    • (2003) FEBS Lett , vol.534 , pp. 115-118
    • Casale, C.H.1    Previtali, G.2    Barra, H.S.3
  • 25
    • 11144224272 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus modulates microtubule dynamics via RhoA-GTP-diaphanous 2 signaling and utilizes the dynein motors to deliver its DNA to the nucleus
    • Naranatt PP, Krishnan HH, Smith MS, Chandran B. 2005. Kaposi's sarcoma-associated herpesvirus modulates microtubule dynamics via RhoA-GTP-diaphanous 2 signaling and utilizes the dynein motors to deliver its DNA to the nucleus. J Virol 79:1191-1206. https://doi.org/10.1128/JVI.79.2.1191-1206.2005.
    • (2005) J Virol , vol.79 , pp. 1191-1206
    • Naranatt, P.P.1    Krishnan, H.H.2    Smith, M.S.3    Chandran, B.4
  • 26
    • 33746658599 scopus 로고    scopus 로고
    • Infection with replicationdeficient adenovirus induces changes in the dynamic instability of host cell microtubules
    • Warren JC, Rutkowski A, Cassimeris L. 2006. Infection with replicationdeficient adenovirus induces changes in the dynamic instability of host cell microtubules. Mol Biol Cell 17:3557-3568. https://doi.org/10.1091/mbc.E05-09-0850.
    • (2006) Mol Biol Cell , vol.17 , pp. 3557-3568
    • Warren, J.C.1    Rutkowski, A.2    Cassimeris, L.3
  • 27
    • 78650919694 scopus 로고    scopus 로고
    • Enhanced acetylation of alpha-tubulin in influenza A virus infected epithelial cells
    • Husain M, Harrod KS. 2011. Enhanced acetylation of alpha-tubulin in influenza A virus infected epithelial cells. FEBS Lett 585:128-132. https://doi.org/10.1016/j.febslet.2010.11.023.
    • (2011) FEBS Lett , vol.585 , pp. 128-132
    • Husain, M.1    Harrod, K.S.2
  • 30
    • 84874715779 scopus 로고    scopus 로고
    • N-terminal phosphorylation of phosphoprotein of vesicular stomatitis virus is required for preventing nucleoprotein from binding to cellular RNAs and for functional template formation
    • Chen L, Zhang S, Banerjee AK, Chen M. 2013. N-terminal phosphorylation of phosphoprotein of vesicular stomatitis virus is required for preventing nucleoprotein from binding to cellular RNAs and for functional template formation. J Virol 87:3177-3186. https://doi.org/10.1128/JVI.02761-12.
    • (2013) J Virol , vol.87 , pp. 3177-3186
    • Chen, L.1    Zhang, S.2    Banerjee, A.K.3    Chen, M.4
  • 31
    • 0034732260 scopus 로고    scopus 로고
    • Precise mapping of the replication and transcription promoters of human parainfluenza virus type 3
    • Hoffman MA, Banerjee AK. 2000. Precise mapping of the replication and transcription promoters of human parainfluenza virus type 3. Virology 269:201-211. https://doi.org/10.1006/viro.2000.0223.
    • (2000) Virology , vol.269 , pp. 201-211
    • Hoffman, M.A.1    Banerjee, A.K.2
  • 32
    • 14544300928 scopus 로고    scopus 로고
    • Virus factories: associations of cell organelles for viral replication and morphogenesis
    • Novoa RR, Calderita G, Arranz R, Fontana J, Granzow H, Risco C. 2005. Virus factories: associations of cell organelles for viral replication and morphogenesis. Biol Cell 97:147-172. https://doi.org/10.1042/BC20040058.
    • (2005) Biol Cell , vol.97 , pp. 147-172
    • Novoa, R.R.1    Calderita, G.2    Arranz, R.3    Fontana, J.4    Granzow, H.5    Risco, C.6


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