Hemolytic activity of the envelope glycoproteins of western equine encephalitis virus in reconstitution experiments

Yamamoto, Kiichi; Suzuki, Kazuo; Simmu, B.

doi:10.1016/0042-6822(81)90518-3

Cited by 14 publications

(14 citation statements)

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“…The haemolytic activity of the virus was clearly located on the E1 glycoprotein and was physically distinct from, although functionally dependent on, the haemagglutinating activity of the protein. This has been reported for the alphavirus of Western equine encephalitis in reconstitution experiments (Yamamoto et al, 1981). The detection of the E1 polypeptide, by indirect immunofluorescence, in the perinuclear region of the cytoplasm using the monoclonal antibodies is in accord with previous reports of the early intracellular location of alphavirus glycoproteins (Kh~irihinen & Renkonen 1977;Pruslin & Scherer 1980).…”

Section: Discussionsupporting

confidence: 78%

Monoclonal Antibodies to Sindbis Virus Glycoprotein E1 can Neutralize, Enhance Infectivity, and Independently Inhibit Haemagglutination or Haemolysis

Chañas

Gould

Clegg

et al. 1982

Journal of General Virology

130

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SUMMARYTwo monoclonal antibodies raised against Sindbis virus were shown to be specific for the envelope glycoprotein E1 by radioimmunoprecipitation (RIP). They had a number of contrasting biological properties. One of them was capable of neutralizing virus infectivity and inhibiting haemagglutination, while the other had no significant neutralizing or haemagglutination-inhibiting capability, but did inhibit virus-mediated haemolysis. Both monoclonal antibodies could enhance virus infectivity of Fc receptor-bearing macrophage-like cells when present at suitable dilutions.

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Section: Discussionsupporting

confidence: 78%

Monoclonal Antibodies to Sindbis Virus Glycoprotein E1 can Neutralize, Enhance Infectivity, and Independently Inhibit Haemagglutination or Haemolysis

Chañas

Gould

Clegg

et al. 1982

Journal of General Virology

130

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“…The antibody raised to purified E 1 or E2 protein possessed HI and virus-binding activity. We have reported that the E 1 protein of WEE virus possesses HA activity (6,15). However, recent studies using McAbs showed that not only anti-El but also anti-E2 McAbs inhibits HA activity (2,10,14).…”

Section: Discussionmentioning

confidence: 99%

“…When anti-E 1 and anti-E2 MSp-Abs are raised against E 1 or E2 proteins isolated with a nonionic detergent, NP-40, which is known to usually be harmless to various biological functions, such as HA and hemolytic activity (15), epitopes involved in NT activity might be deformed in such proteins by a conformational change. This suggests that WEE virus contains some antigenic determinants involved in NT which are present only on intact virus particles and are completely destroyed by solubilization of the virion.…”

Section: Discussionmentioning

confidence: 99%

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Properties of Monospecific Antibodies to the Glycoprotein of Western Equine Encephalitis Virus

Yamamoto

1986

Microbiology and Immunology

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Monospecific (MSp-) antisera against E 1 and E2 glycoproteins of western equine encephalitis (WEE) virus were prepared and examined for binding activities to whole virions, hemagglutination-inhibition (HI), neutralization (NT) and protection. Both anti-E l and anti-E2 MSp-antibodies (Abs) showed HI activity, but not NT activity. Both NT-negative MSp-Abs protected mice against WEE virus challenge. A competition experiment with monoclonal antibodies showed that these MSp-antisera appear to lack the antibody population for some epitopes involved in viral neutralization.Western equine encephalitis (WEE) virus belongs to the Alphavirus genus and contains two glycoproteins, E 1 and E2, which are probably present on the virion surface as heterodimeric spikes. These glycoproteins are responsible for the serological grouping of alphaviruses by neutralization (NT) and hemagglutinationinhibition (HI) reactions. However, the precise role of the two glycoproteins in the serological reactions is not well understood even in the case of Sindbis and Semliki Forest viruses which have been widely studied among the alphaviruses (4, 5). Dalrymple et al (4) reported that anti-E2 monospecific antibody (MSp-Ab) to the purified E2 protein of Sindbis virus showed NT activity and that anti-E 1 MSp-Ab showed little NT activity. However, Symington et al (12) demonstrated direct NT activity of anti-E 1 antibody and an enhanced NT reaction with anti-mouse immunoglobulin (IgG) goat serum in both MSp-Abs. Therefore, in the case of the polyclonal antibody to purified envelope glycoprotein, it is not known which MSp-Ab, anti-E 1 or anti-E2, is involved in the NT reaction.With respect to HI activity, only anti-E 1 MSp-Ab shows HI activity (4). Recent studies with monoclonal antibodies (McAbs) revealed that not only anti-E 1 but also anti-E2 McAb possesses HI activity (2,10,14). However, there is sometimes an increase in production of McAbs against rare antigenic determinant sites which are not usually recognized in conventional immunization such as vaccination or during convalescence from viral infection. Therefore, the HI activity of anti-E2 343

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“…In Sindbis virus-infected cells, the P62-El complex has fusion activity. Isolated preparations of E l from Western equine encephalitis virus reconstituted into lipid bilayers are able to lyse erythrocytes (Yamamoto et al, 1981). Antibodies specific to E l can inhibit fusion (Chanas et al, 19821, and monoclonal antibodies have been found that recognize an E l epitope appearing after low pH (Schmaljohn et al, 1983).…”

Section: Fusion Activitymentioning

confidence: 99%

Domains of Virus Glycoproteins

Schlesinger

1987

Advances in Virus Research

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Hemolytic activity of the envelope glycoproteins of western equine encephalitis virus in reconstitution experiments

Cited by 14 publications

References 13 publications

Monoclonal Antibodies to Sindbis Virus Glycoprotein E1 can Neutralize, Enhance Infectivity, and Independently Inhibit Haemagglutination or Haemolysis

Monoclonal Antibodies to Sindbis Virus Glycoprotein E1 can Neutralize, Enhance Infectivity, and Independently Inhibit Haemagglutination or Haemolysis

Properties of Monospecific Antibodies to the Glycoprotein of Western Equine Encephalitis Virus

Domains of Virus Glycoproteins

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