Structure-antigenicity of the V3 region of SIVmac envelope glycoprotein.
The objective of this study was to analyze the immunogenicity and antigenicity of the V3 domain (Cys313-Cys346) of the external envelope glycoprotein gp125 of SIVmac251. The corresponding peptide was synthesized and characterized as linear and cyclic peptides. Our results showed that this region, as for HIV-1, contained an immunodominant epitope. The antigenicity was similar for the linear and cyclic peptides when tested against a panel of 15 sera from SIV infected macaques. Similarly, both peptide structures presented similar immunogenicity as shown by the characterization of the anti-peptide antibodies produced in rabbits against the cyclic and linear forms. But, unexpectedly, the antibodies produced against linear peptides recognized with a relatively higher intensity the native envelope gp140 than those produced against the cyclic structure. Furthermore, we showed that these antibodies recognized better the deglycosylated form of the glycoprotein. But, in contrast to the neutralizing activity obtained with anti-V3 peptides from HIV-1, no antiviral activity was obtained with antibodies generated against linear or cyclic SIVmac V3 peptides.
Gaston
Fabrice
F
Laboratoire d'immuno-virologie, Université Paul Sabatier, UFR/SVT, 31062 Toulouse, France. gaston@cict.fr
Babas
Tahar
T
Lakhdar-Ghazal
Faouzi
F
Bahraoui
Elmostafa
E
D000478:Alkylation; D000595:Amino Acid Sequence; D000818:Animals; D002460:Cell Line; D004797:Enzyme-Linked Immunosorbent Assay; D006023:Glycoproteins / Q000737:chemistry* / Q000276:immunology*; D016056:Immunodominant Epitopes; D008969:Molecular Sequence Data; D011817:Rabbits; D011863:Radioimmunoassay; D015302:Simian Immunodeficiency Virus / Q000737:chemistry*; D013329:Structure-Activity Relationship; D014759:Viral Envelope Proteins / Q000737:chemistry* / Q000276:immunology*
D006023:Glycoproteins; D016056:Immunodominant Epitopes; D014759:Viral Envelope Proteins