Transmembrane domain of influenza virus neuraminidase, a type II protein, possesses an apical sorting signal in polarized MDCK cells - PubMed (original) (raw)
Transmembrane domain of influenza virus neuraminidase, a type II protein, possesses an apical sorting signal in polarized MDCK cells
A Kundu et al. J Virol. 1996 Sep.
Abstract
The influenza virus neuraminidase (NA), a type II transmembrane protein, is directly transported to the apical plasma membrane in polarized MDCK cells. By using deletion mutants and chimeric constructs of influenza virus NA with the human transferrin receptor, a type II basolateral transmembrane protein, we investigated the location of the apical sorting signal of influenza virus NA. When these mutant and chimeric proteins were expressed in stably transfected polarized MDCK cells, the transmembrane domain of NA, and not the cytoplasmic tail, provided a determinant for apical targeting in polarized MDCK cells and this transmembrane signal was sufficient for sorting and transport of the ectodomain of a reporter protein (transferrin receptor) directly to the apical plasma membrane of polarized MDCK cells. In addition, by using differential detergent extraction, we demonstrated that influenza virus NA and the chimeras which were transported to the apical plasma membrane also became insoluble in Triton X-100 but soluble in octylglucoside after extraction from MDCK cells during exocytic transport. These data indicate that the transmembrane domain of NA provides the determinant(s) both for apical transport and for association with Triton X-100-insoluble lipids.
Similar articles
- Analysis of the transmembrane domain of influenza virus neuraminidase, a type II transmembrane glycoprotein, for apical sorting and raft association.
Barman S, Nayak DP. Barman S, et al. J Virol. 2000 Jul;74(14):6538-45. doi: 10.1128/jvi.74.14.6538-6545.2000. J Virol. 2000. PMID: 10864667 Free PMC article. - Transport of viral proteins to the apical membranes and interaction of matrix protein with glycoproteins in the assembly of influenza viruses.
Barman S, Ali A, Hui EK, Adhikary L, Nayak DP. Barman S, et al. Virus Res. 2001 Sep;77(1):61-9. doi: 10.1016/s0168-1702(01)00266-0. Virus Res. 2001. PMID: 11451488 Review. - Differential detergent resistance of the apical and basolateral NPPases: relationship with polarized targeting.
Delaunay JL, Breton M, Goding JW, Trugnan G, Maurice M. Delaunay JL, et al. J Cell Sci. 2007 Mar 15;120(Pt 6):1009-16. doi: 10.1242/jcs.002717. Epub 2007 Feb 20. J Cell Sci. 2007. PMID: 17311850 - Influenza virus morphogenesis and budding.
Nayak DP, Balogun RA, Yamada H, Zhou ZH, Barman S. Nayak DP, et al. Virus Res. 2009 Aug;143(2):147-61. doi: 10.1016/j.virusres.2009.05.010. Epub 2009 May 27. Virus Res. 2009. PMID: 19481124 Free PMC article. Review.
Cited by
- Residues in the hendra virus fusion protein transmembrane domain are critical for endocytic recycling.
Popa A, Carter JR, Smith SE, Hellman L, Fried MG, Dutch RE. Popa A, et al. J Virol. 2012 Mar;86(6):3014-26. doi: 10.1128/JVI.05826-11. Epub 2012 Jan 11. J Virol. 2012. PMID: 22238299 Free PMC article. - Rafts promote assembly and atypical targeting of a nonenveloped virus, rotavirus, in Caco-2 cells.
Sapin C, Colard O, Delmas O, Tessier C, Breton M, Enouf V, Chwetzoff S, Ouanich J, Cohen J, Wolf C, Trugnan G. Sapin C, et al. J Virol. 2002 May;76(9):4591-602. doi: 10.1128/jvi.76.9.4591-4602.2002. J Virol. 2002. PMID: 11932424 Free PMC article. - Reovirus FAST protein transmembrane domains function in a modular, primary sequence-independent manner to mediate cell-cell membrane fusion.
Clancy EK, Duncan R. Clancy EK, et al. J Virol. 2009 Apr;83(7):2941-50. doi: 10.1128/JVI.01869-08. Epub 2009 Jan 7. J Virol. 2009. PMID: 19129451 Free PMC article. - Rotavirus is released from the apical surface of cultured human intestinal cells through nonconventional vesicular transport that bypasses the Golgi apparatus.
Jourdan N, Maurice M, Delautier D, Quero AM, Servin AL, Trugnan G. Jourdan N, et al. J Virol. 1997 Nov;71(11):8268-78. doi: 10.1128/JVI.71.11.8268-8278.1997. J Virol. 1997. PMID: 9343179 Free PMC article. - Association of influenza virus NP and M1 proteins with cellular cytoskeletal elements in influenza virus-infected cells.
Avalos RT, Yu Z, Nayak DP. Avalos RT, et al. J Virol. 1997 Apr;71(4):2947-58. doi: 10.1128/JVI.71.4.2947-2958.1997. J Virol. 1997. PMID: 9060654 Free PMC article.
References
- Nature. 1970 Aug 15;227(5259):680-5 - PubMed
- Proc Natl Acad Sci U S A. 1988 Dec;85(24):9557-61 - PubMed
- Proc Natl Acad Sci U S A. 1978 Oct;75(10):5071-5 - PubMed
- Cell. 1980 May;20(1):45-54 - PubMed
- J Virol. 1983 Mar;45(3):1065-73 - PubMed
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources