Structure, Function, and Antigenicity of the Hemagglutinin of Influenza Virus

Wharton, Steve; Weis, William I.; Skehel, J.J.; Wiley, Don C.

doi:10.1007/978-1-4613-0811-9_3

Cited by 34 publications

(24 citation statements)

References 73 publications

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“…The CRU is N-acetylneuraminic acid (NANA), and on RBCs most NANA is present on glycophorin A. The VAS is a pocket in the distal part of each HA monomer (Wilson et al, 1981 ;Wharton et al, 1989). HI antibody sterically prevents the interactions between the VAS and the CRU, and the attachment of the virion to the RBC.…”

Section: Haemagglutination-inhibitionmentioning

confidence: 99%

Variations in the neutralizing and haemagglutination-inhibiting activities of five influenza A virus-specific IgGs and their antibody fragments.

Schofield

Stephenson

Dimmock

1997

Journal of General Virology

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Neutralization and haemagglutination-inhibition (HI) of a type A influenza virus by a panel of five monoclonal IgGs, their F(abh) 2 s, Fabs and FabsM anti-mouse Fab were compared. The MAbs were specific for antigenic sites A, B and D of the haemagglutinin. Activities of the IgGs varied by up to 6-fold on a molar basis, apart from the HI activity of HC58 which was 100-fold lower. This was not due to low functional affinity as HC58 had the second highest value (nM) as determined by an equilibrium method with whole virions. Conversion to the F(abh) 2 reduced neutralization and HI by only 2-to 6-fold, indicating that the Fc region had little involvement in these processes. However, all Fabs had low neutralization and HI activity compared with their IgGs, neutralization being reduced by 86

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Section: Haemagglutination-inhibitionmentioning

confidence: 99%

Variations in the neutralizing and haemagglutination-inhibiting activities of five influenza A virus-specific IgGs and their antibody fragments.

Schofield

Stephenson

Dimmock

1997

Journal of General Virology

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“…He incubated red cells with virus, observed the hemagglutination reaction, and noticed that with the passage of time the reaction was not sustained. One of the 2 surface glycoproteins of the virus, the hemagglutinin (reviewed by Wharton et al, 1989), binds to red cells via sialic acid-containing glycoconjugates on the red cell surface. The other surface glycoprotein, the neuraminidase (reviewed by Colman, 1989), specifically liberates sialic acid (N-acetyl neuraminic acid, NeuSAc, Fig.…”

mentioning

confidence: 99%

Influenza virus neuraminidase: Structure, antibodies, and inhibitors

Colman¹

1994

Protein Science

314

224

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The determination of the 3-dimensional structure of the influenza virus neuraminidase in 1983 has served as a platform for understanding interactions between antibodies and protein antigens, for investigating antigenic variation in influenza viruses, and for devising new inhibitors of the enzyme. That work is reviewed here, together with more recent developments that have resulted in one of the inhibitors entering clinical trials as an anti-influenza virus drug.

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“…Cellular receptor-binding proteins usually contain highly conserved domains that mediate specific interactions with cellular components (23,24). These conserved regions, usually inaccessible to antibody binding, are often surrounded by variable regions that allow viruses to escape from the immune response (23,24).…”

Section: Discussionmentioning

confidence: 99%

Production and characterization of monoclonal antibodies to Brazilian isolates of bovine viral diarrhea virus

Kreutz

Donis

Gil

et al. 2000

Braz J Med Biol Res

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Three Brazilian isolates of bovine viral diarrhea virus (BVDV), antigenically distinct from the standard North American isolates, were selected to immunize BALB/c mice in order to obtain hybridoma cells secreting anti-BVDV monoclonal antibodies (mAbs). Two hybridoma clones secreting mAbs, reacting specifically with BVDV-infected cells (mAbs 3.1C4 and 6.F11), were selected after five fusions and screening of 1001 hypoxanthine-aminopterin-thymidine-resistant clones. These mAbs reacted in an indirect fluorescent antibody (IFA) assay with all 39 South and North American BVDV field isolates and reference strains available in our laboratory, yet failed to recognize other pestiviruses, namely the hog cholera virus. The mAbs reacted at dilutions up to 1:25,600 (ascitic fluid) and 1:100 (hybridoma culture supernatant) in IFA and immunoperoxidase (IPX) staining of BVDVinfected cells but only mAb 3.1C4 neutralized virus infectivity. Furthermore, both mAbs failed to recognize BVDV proteins by IPX in formalin-fixed paraffin-embedded tissues and following SDS-PAGE and immunoblot analysis of virus-infected cells, suggesting they are probably directed to conformational-type epitopes. The protein specificity of these mAbs was then determined by IFA staining of CV-1 cells transiently expressing each of the BVDV proteins: mAb 3.1C4 reacted with the structural protein E2/gp53 and mAb 6.F11 reacted with the structural protein E1/gp25. Both mAbs were shown to be of the IgG2a isotype. To our knowledge, these are the first mAbs produced against South American BVDV isolates and will certainly be useful for research and diagnostic purposes.

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Structure, Function, and Antigenicity of the Hemagglutinin of Influenza Virus

Cited by 34 publications

References 73 publications

Variations in the neutralizing and haemagglutination-inhibiting activities of five influenza A virus-specific IgGs and their antibody fragments.

Variations in the neutralizing and haemagglutination-inhibiting activities of five influenza A virus-specific IgGs and their antibody fragments.

Influenza virus neuraminidase: Structure, antibodies, and inhibitors

Production and characterization of monoclonal antibodies to Brazilian isolates of bovine viral diarrhea virus

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