scholarly journals Antibodies specific for hypervariable regions 3 to 5 of the feline immunodeficiency virus envelope glycoprotein are not solely responsible for vaccine-induced acceleration of challenge infection in cats

2004 ◽  
Vol 85 (7) ◽  
pp. 1833-1841 ◽  
Author(s):  
Willem Huisman ◽  
Eefje J. A. Schrauwen ◽  
Suzan D. Pas ◽  
Jos A. Karlas ◽  
Guus F. Rimmelzwaan ◽  
...  
Keyword(s):  
Feline Immunodeficiency Virus ◽  
Envelope Glycoprotein ◽  
Challenge Infection ◽  
Antibody Responses ◽  
Causative Role ◽  
Virus Envelope ◽  
Humoral Immune ◽  
Hypervariable Regions ◽  
Immunodeficiency Virus

In a previous vaccination study in cats, the authors reported on accelerated feline immunodeficiency virus (FIV) replication upon challenge in animals vaccinated with a candidate envelope subunit vaccine. Plasma transfer studies as well as antibody profiles in vaccinated cats indicated a causative role for antibodies directed against the hypervariable regions HV3, HV4 and HV5 (HV3–5) of the envelope glycoprotein. The present study was designed to investigate further the contribution of antibodies in envelope vaccine-induced acceleration of FIV infection. To this end, regions HV3–5 of the envelope glycoprotein were deleted from the original vaccine, thus addressing the contributing role of antibodies directed against these hypervariable regions. Interestingly, this approach did not prevent acceleration of challenge infection. Analysis of the antibody responses in the respective groups suggested that removal of HV3–5 redirected the humoral immune response towards other regions of the envelope glycoprotein, indicating that these regions can also induce antibodies that accelerate virus replication.

scholarly journals Mechanism of feline immunodeficiency virus envelope glycoprotein-mediated fusion

Virology ◽  
2004 ◽  
Vol 321 (2) ◽  
pp. 274-286 ◽  
Author(s):  
Himanshu Garg ◽  
Frederick J. Fuller ◽  
Wayne A.F. Tompkins
Keyword(s):  
Feline Immunodeficiency Virus ◽  
Envelope Glycoprotein ◽  
Virus Envelope ◽  
Immunodeficiency Virus

scholarly journals Role of N-Linked Glycans in a Human Immunodeficiency Virus Envelope Glycoprotein: Effects on Protein Function and the Neutralizing Antibody Response

2002 ◽  
Vol 76 (9) ◽  
pp. 4199-4211 ◽  
Author(s):  
Miriam I. Quiñones-Kochs ◽  
Linda Buonocore ◽  
John K. Rose
Keyword(s):  
Human Immunodeficiency Virus ◽  
Envelope Glycoprotein ◽  
Protein Function ◽  
Neutralizing Antibodies ◽  
Immune Recognition ◽  
Wild Type ◽  
Virus Envelope ◽  
Mutant Proteins ◽  
Immunodeficiency Virus

ABSTRACT The envelope (Env) glycoprotein of human immunodeficiency virus (HIV) contains 24 N-glycosylation sites covering much of the protein surface. It has been proposed that one role of these carbohydrates is to form a shield that protects the virus from immune recognition. Strong evidence for such a role for glycosylation has been reported for simian immunodeficiency virus (SIV) mutants lacking glycans in the V1 region of Env (J. N. Reitter, R. E. Means, and R. C. Desrosiers, Nat. Med. 4:679-684, 1998). Here we used recombinant vesicular stomatitis viruses (VSVs) expressing HIV Env glycosylation mutants to determine if removal of carbohydrates in the V1 and V2 domains affected protein function and the generation of neutralizing antibodies in mice. Mutations that eliminated one to six of the sites for N-linked glycosylation in the V1 and V2 loops were introduced into a gene encoding the HIV type 1 primary isolate 89.6 envelope glycoprotein with its cytoplasmic domain replaced by that of the VSV G glycoprotein. The membrane fusion activities of the mutant proteins were studied in a syncytium induction assay. The transport and processing of the mutant proteins were studied with recombinant VSVs expressing mutant Env G proteins. We found that HIV Env V1 and V2 glycosylation mutants were no better than wild-type envelope at inducing antibodies neutralizing wild-type Env, although an Env mutant lacking glycans appeared somewhat more sensitive to neutralization by antibodies raised to mutant or wild-type Env. These results indicate significant differences between SIV and HIV with regard to the roles of glycans in the V1 and V2 domains.

scholarly journals Structural characterization of the feline-immunodeficiency-virus envelope glycoprotein 36 ectodomain for the development of new antivirals

2005 ◽  
Vol 389 (2) ◽  
pp. 559-567 ◽  
Author(s):  
Florestan Desmaris ◽  
David Lemaire ◽  
Sylvie Ricard-Blum ◽  
Benoît Chatrenet ◽  
Eric Forest
Keyword(s):  
Feline Immunodeficiency Virus ◽  
Envelope Glycoprotein ◽  
Analytical Ultracentrifugation ◽  
Structural Data ◽  
Structural Features ◽  
Terminal Region ◽  
Amino Acid Residues ◽  
Virus Envelope ◽  
Fusion Inhibitors ◽  
Immunodeficiency Virus

In the fight against the human HIV, new targets are being explored, such as the proteins involved in the process of fusion of the virus with the host cell. Recently, the first generation of fusion inhibitors (enfuvirtide), targeting gp41 (virus envelope glycoprotein 41), has become commercially available. However, this promising class of drugs has to be improved in respect of their efficacy and bioavailability. Considering the strong homologies between HIV and FIV (feline immunodeficiency virus), as well as the highly conserved structure of the transmembrane envelope protein among species, FIV represents a relevant model of pre-screening studies for HIV. Taking into account (i) sequence homologies between the ectodomain of HIV gp41 and FIV gp36 (envelope glycoprotein 36), (ii) structural data available for gp41 and (iii) the fact that synthetic peptides derived from gp36 are effective inhibitors of FIV infection, we designed several peptides derived from gp36 sequence. We checked that these peptides had the same structural features as the corresponding peptides from gp41 HIV by CD, analytical ultracentrifugation and 1H–2H (hydrogen–deuterium) exchange combined with MS. By combining this latter technique with surface-plasmon-resonance assays, we identified the amino acid residues of the C-terminal region of the ectodomain of gp36 that are critical for interaction with the N-terminal region. This gave clues for therapy and vaccines against FIV, thus providing helpful data for treatments against HIV.

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