Literature DB >> 6193286

Monoclonal anti-hemagglutinin antibodies detect irreversible antigenic alterations that coincide with the acid activation of influenza virus A/PR/834-mediated hemolysis.

J W Yewdell, W Gerhard, T Bachi.   

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.

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Year:  1983        PMID: 6193286      PMCID: PMC255340     

Source DB:  PubMed          Journal:  J Virol        ISSN: 0022-538X            Impact factor:   5.103


  21 in total

1.  Enhancement of the infectivity of influenza A and B viruses by proteolytic cleavage of the hemagglutinin polypeptide.

Authors:  S G Lazarowitz; P W Choppin
Journal:  Virology       Date:  1975-12       Impact factor: 3.616

2.  Activation of influenza A viruses by trypsin treatment.

Authors:  H D Klenk; R Rott; M Orlich; J Blödorn
Journal:  Virology       Date:  1975-12       Impact factor: 3.616

3.  Purification of the fusion protein of Sendai virus: analysis of the NH2-terminal sequence generated during precursor activation.

Authors:  M J Gething; J M White; M D Waterfield
Journal:  Proc Natl Acad Sci U S A       Date:  1978-06       Impact factor: 11.205

4.  Structural identification of the antibody-binding sites of Hong Kong influenza haemagglutinin and their involvement in antigenic variation.

Authors:  D C Wiley; I A Wilson; J J Skehel
Journal:  Nature       Date:  1981-01-29       Impact factor: 49.962

5.  Influenza viruses cause hemolysis and fusion of cells.

Authors:  R T Huang; R Rott; H D Klenk
Journal:  Virology       Date:  1981-04-15       Impact factor: 3.616

6.  Activation of influenza virus by acidic media causes hemolysis and fusion of erythrocytes.

Authors:  T Maeda; S Ohnishi
Journal:  FEBS Lett       Date:  1980-12-29       Impact factor: 4.124

7.  Studies on the mechanism of influenza virus entry into cells.

Authors:  S Patterson; J S Oxford; R R Dourmashkin
Journal:  J Gen Virol       Date:  1979-04       Impact factor: 3.891

8.  Changes in the antigenicity of the hemagglutinin molecule of H3 influenza virus at acidic pH.

Authors:  R G Webster; L E Brown; D C Jackson
Journal:  Virology       Date:  1983-04-30       Impact factor: 3.616

9.  The analysis of the monoclonal immune response to influenza virus. II. The antigenicity of the viral hemagglutinin.

Authors:  W Gerhard
Journal:  J Exp Med       Date:  1976-10-01       Impact factor: 14.307

10.  Disquisitions of Original Antigenic Sin. I. Evidence in man.

Authors:  R G Webster
Journal:  J Exp Med       Date:  1966-09-01       Impact factor: 14.307

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  40 in total

1.  Hemagglutinin 1-specific immunoglobulin G and Fab molecules mediate postattachment neutralization of influenza A virus by inhibition of an early fusion event.

Authors:  M J Edwards; N J Dimmock
Journal:  J Virol       Date:  2001-11       Impact factor: 5.103

2.  Investigation of pathways for the low-pH conformational transition in influenza hemagglutinin.

Authors:  M Madhusoodanan; Themis Lazaridis
Journal:  Biophys J       Date:  2003-03       Impact factor: 4.033

3.  Activation of fusion by the SER virus F protein: a low-pH-dependent paramyxovirus entry process.

Authors:  Shaguna Seth; Annelet Vincent; R W Compans
Journal:  J Virol       Date:  2003-06       Impact factor: 5.103

4.  Glycoprotein B of herpes simplex virus 2 has more than one intracellular conformation and is altered by low pH.

Authors:  Martin I Muggeridge
Journal:  J Virol       Date:  2012-04-18       Impact factor: 5.103

5.  Intermonomer disulfide bonds impair the fusion activity of influenza virus hemagglutinin.

Authors:  G W Kemble; D L Bodian; J Rosé; I A Wilson; J M White
Journal:  J Virol       Date:  1992-08       Impact factor: 5.103

6.  An analysis of the properties of monoclonal antibodies directed to epitopes on influenza virus hemagglutinin.

Authors:  L E Brown; J M Murray; D O White; D C Jackson
Journal:  Arch Virol       Date:  1990       Impact factor: 2.574

7.  Influenza A virus hemagglutinin trimerization completes monomer folding and antigenicity.

Authors:  Javier G Magadán; Surender Khurana; Suman R Das; Gregory M Frank; James Stevens; Hana Golding; Jack R Bennink; Jonathan W Yewdell
Journal:  J Virol       Date:  2013-07-03       Impact factor: 5.103

8.  Is bivalent binding of monoclonal antibodies to different antigenic areas on the hemagglutinin of influenza virus required for neutralization of viral infectivity?

Authors:  S Yoden; H Kida; R Yanagawa
Journal:  Arch Virol       Date:  1985       Impact factor: 2.574

9.  Monoclonal antibodies detect different forms of influenza virus hemagglutinin during viral penetration and biosynthesis.

Authors:  T Bächi; W Gerhard; J W Yewdell
Journal:  J Virol       Date:  1985-08       Impact factor: 5.103

10.  Mutations in or near the fusion peptide of the influenza virus hemagglutinin affect an antigenic site in the globular region.

Authors:  J W Yewdell; A Taylor; A Yellen; A Caton; W Gerhard; T Bächi
Journal:  J Virol       Date:  1993-02       Impact factor: 5.103

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