Monoclonal anti-hemagglutinin antibodies detect irreversible antigenic alterations that coincide with the acid activation of influenza virus A/PR/834-mediated hemolysis
- PMID: 6193286
- PMCID: PMC255340
- DOI: 10.1128/JVI.48.1.239-248.1983
Monoclonal anti-hemagglutinin antibodies detect irreversible antigenic alterations that coincide with the acid activation of influenza virus A/PR/834-mediated hemolysis
Abstract
Exposure of influenza virus to an acidic environment, which is known to be required for viral fusion and hemolysis, has recently been shown to induce a conformational change in the hemagglutinin molecule. In the present study, we examined the effects of acid incubation on the antigenicity, biological activity, and morphology of influenza virus A/PR/8/34 (H1N1). Incubation of PR8 virus at pH 5 in the absence of erythrocytes resulted in a rapid and irreversible loss of viral hemolytic activity and infectivity. Apart from a less distinct appearance of the viral surface projections and slight damage to the envelope structure, acid incubation did not result in gross morphological changes in the viral architecture. The acid-induced change could be detected in the form of greatly increased or decreased binding of many monoclonal antibodies directed to each of the four major antigenic regions of the hemagglutinin. Triggering of viral hemolytic activity and antigenic alterations was similarly pH dependent. In addition, the different pH dependencies of egg-grown and trypsin-treated MDCK-grown viruses coincided with an analogous pH dependence of the antigenic alterations that were observed with these viruses. These observations are compatible with the idea that some of the anti-hemagglutinin antibodies detect conformational changes in the hemagglutinin which are required for the initiation of fusion and hemolysis.
Similar articles
-
Inhibition of virus-induced hemolysis with monoclonal antibodies to different antigenic areas on the hemagglutinin molecule of A/seal/Massachusetts/1/80 (H7N7) influenza virus.Arch Virol. 1983;76(2):91-9. doi: 10.1007/BF01311693. Arch Virol. 1983. PMID: 6191738
-
Antigenic determinants of influenza virus hemagglutinin. XI. Conformational changes detected by monoclonal antibodies.Virology. 1985 Aug;145(1):72-83. doi: 10.1016/0042-6822(85)90202-8. Virology. 1985. PMID: 2409671
-
Is bivalent binding of monoclonal antibodies to different antigenic areas on the hemagglutinin of influenza virus required for neutralization of viral infectivity?Arch Virol. 1985;85(3-4):209-16. doi: 10.1007/BF01314232. Arch Virol. 1985. PMID: 2411245
-
Changes in the antigenicity of the hemagglutinin molecule of H3 influenza virus at acidic pH.Virology. 1983 Apr 30;126(2):587-99. doi: 10.1016/s0042-6822(83)80015-4. Virology. 1983. PMID: 6190310
-
Monoclonal antibodies detect different forms of influenza virus hemagglutinin during viral penetration and biosynthesis.J Virol. 1985 Aug;55(2):307-13. doi: 10.1128/JVI.55.2.307-313.1985. J Virol. 1985. PMID: 2410628 Free PMC article.
Cited by
-
Recent advances in "universal" influenza virus antibodies: the rise of a hidden trimeric interface in hemagglutinin globular head.Front Med. 2020 Apr;14(2):149-159. doi: 10.1007/s11684-020-0764-y. Epub 2020 Apr 1. Front Med. 2020. PMID: 32239416 Free PMC article. Review.
-
Immunogenicity of low-pH treated whole viral influenza vaccine.Virology. 2011 Aug 15;417(1):196-202. doi: 10.1016/j.virol.2011.05.014. Epub 2011 Jun 30. Virology. 2011. PMID: 21722934 Free PMC article.
-
Canonical features of human antibodies recognizing the influenza hemagglutinin trimer interface.J Clin Invest. 2021 Aug 2;131(15):e146791. doi: 10.1172/JCI146791. J Clin Invest. 2021. PMID: 34156974 Free PMC article.
-
Anti-peptide antibodies detect steps in a protein conformational change: low-pH activation of the influenza virus hemagglutinin.J Cell Biol. 1987 Dec;105(6 Pt 2):2887-96. doi: 10.1083/jcb.105.6.2887. J Cell Biol. 1987. PMID: 2447101 Free PMC article.
-
Inactivation mechanisms of influenza A virus under pH conditions encountered in aerosol particles as revealed by whole-virus HDX-MS.mSphere. 2023 Oct 24;8(5):e0022623. doi: 10.1128/msphere.00226-23. Epub 2023 Aug 18. mSphere. 2023. PMID: 37594288 Free PMC article.
References
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Research Materials