Structure and assembly of hemagglutinin mutants of fowl plague virus with impaired surface transport - PubMed (original) (raw)
Structure and assembly of hemagglutinin mutants of fowl plague virus with impaired surface transport
W Garten et al. J Virol. 1992 Mar.
Abstract
Five temperature-sensitive mutants of influenza virus A/FPV/Rostock/34 (H7N1), ts206, ts293, ts478, ts482, and ts651, displaying correct hemagglutinin (HA) insertion into the apical plasma membrane of MDCK cells at the permissive temperature but defective transport to the cell surface at the restrictive temperature, have been investigated. Nucleotide sequence analysis of the HA gene of the mutants and their revertants demonstrated that with each mutant a single amino acid change is responsible for the transport block. The amino acid substitutions were compared with those of mutants ts1 and ts227, which have been analyzed previously (W. Schuy, C. Will, K. Kuroda, C. Scholtissek, W. Garten, and H.-D. Klenk, EMBO J. 5:2831-2836, 1986). With the exception of ts206, the changed amino acids of all mutants and revertants accumulate in three distinct areas of the three-dimensional HA model: (i) at the tip of the 80-A (8-nm)-long alpha helix, (ii) at the connection between the globular region and stem, and (iii) in the basal domain of the stem. The concept that these areas are critical for HA assembly and hence for transport is supported by the finding that the mutants that are unable to leave the endoplasmic reticulum at the nonpermissive temperature do not correctly trimerize. Upon analysis by density gradient centrifugation, cross-linking, and digestion with trypsin and endoglucosaminidase H, two groups can be discriminated among these mutants: with ts1, ts227, and ts478, the HA forms large irreversible aggregates, whereas with ts206 and ts293, it is retained in the monomeric form in the endoplasmic reticulum. With a third group, comprising mutants ts482 and ts651 that enter the Golgi apparatus, trimerization was not impaired.
Similar articles
- Temperature-sensitive mutants of fowl plague virus defective in the intracellular transport of the hemagglutinin.
Naruse H, Scholtissek C, Klenk HD. Naruse H, et al. Virus Res. 1986 Aug;5(2-3):293-305. doi: 10.1016/0168-1702(86)90025-0. Virus Res. 1986. PMID: 3765827 - Mutations blocking the transport of the influenza virus hemagglutinin between the rough endoplasmic reticulum and the Golgi apparatus.
Schuy W, Will C, Kuroda K, Scholtissek C, Garten W, Klenk HD. Schuy W, et al. EMBO J. 1986 Nov;5(11):2831-6. doi: 10.1002/j.1460-2075.1986.tb04576.x. EMBO J. 1986. PMID: 3024963 Free PMC article. - Role of conserved glycosylation sites in maturation and transport of influenza A virus hemagglutinin.
Roberts PC, Garten W, Klenk HD. Roberts PC, et al. J Virol. 1993 Jun;67(6):3048-60. doi: 10.1128/JVI.67.6.3048-3060.1993. J Virol. 1993. PMID: 8497042 Free PMC article. - Expression of wild-type and mutant forms of influenza hemagglutinin: the role of folding in intracellular transport.
Gething MJ, McCammon K, Sambrook J. Gething MJ, et al. Cell. 1986 Sep 12;46(6):939-50. doi: 10.1016/0092-8674(86)90076-0. Cell. 1986. PMID: 3757030 - Influenza virus M2 protein and haemagglutinin conformation changes during intracellular transport.
Ciampor F, Cmarko D, Cmarková J, Závodská E. Ciampor F, et al. Acta Virol. 1995 Jun;39(3):171-81. Acta Virol. 1995. PMID: 8579000 Review.
Cited by
- Substitution Arg140Gly in Hemagglutinin Reduced the Virulence of Highly Pathogenic Avian Influenza Virus H7N1.
Treshchalina A, Postnikova Y, Boravleva E, Gambaryan A, Belyakova A, Ishmukhametov A, Sadykova G, Prilipov A, Lomakina N. Treshchalina A, et al. Viruses. 2021 Aug 11;13(8):1584. doi: 10.3390/v13081584. Viruses. 2021. PMID: 34452449 Free PMC article. - Modulation of cell surface transport and lipid raft localization by the cytoplasmic tail of the influenza virus hemagglutinin.
Scolari S, Imkeller K, Jolmes F, Veit M, Herrmann A, Schwarzer R. Scolari S, et al. Cell Microbiol. 2016 Jan;18(1):125-36. doi: 10.1111/cmi.12491. Epub 2015 Aug 31. Cell Microbiol. 2016. PMID: 26243691 Free PMC article. - Hemagglutinin-esterase-fusion (HEF) protein of influenza C virus.
Wang M, Veit M. Wang M, et al. Protein Cell. 2016 Jan;7(1):28-45. doi: 10.1007/s13238-015-0193-x. Epub 2015 Jul 28. Protein Cell. 2016. PMID: 26215728 Free PMC article. Review. - The Lassa virus glycoprotein precursor GP-C is proteolytically processed by subtilase SKI-1/S1P.
Lenz O, ter Meulen J, Klenk HD, Seidah NG, Garten W. Lenz O, et al. Proc Natl Acad Sci U S A. 2001 Oct 23;98(22):12701-5. doi: 10.1073/pnas.221447598. Epub 2001 Oct 16. Proc Natl Acad Sci U S A. 2001. PMID: 11606739 Free PMC article. - Elongation of the cytoplasmic tail interferes with the fusion activity of influenza virus hemagglutinin.
Ohuchi M, Fischer C, Ohuchi R, Herwig A, Klenk HD. Ohuchi M, et al. J Virol. 1998 May;72(5):3554-9. doi: 10.1128/JVI.72.5.3554-3559.1998. J Virol. 1998. PMID: 9557635 Free PMC article.
References
- Vaccine. 1985 Sep;3(3 Suppl):227-9 - PubMed
- J Cell Biol. 1986 Oct;103(4):1179-91 - PubMed
- J Gen Virol. 1985 Aug;66 ( Pt 8):1687-95 - PubMed
- Cell. 1985 Feb;40(2):431-9 - PubMed
- J Cell Biol. 1988 Jul;107(1):89-99 - PubMed
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources