Collect. Czech. Chem. Commun.
1995, 60, 1054-1064
https://doi.org/10.1135/cccc19951054
Time Dependence of Immunoresponse of Different Epitopes of gp41 and Its Relation to the Structure of Short Peptide Fragments of gp41
Dalibor Štysa,b, Ján Novákc, Viktor Krchňákd,e, Josef Vágnerd, Petr Štropa,e and Miloš Buděšínskýa
a Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 166 10 Prague 6, Czech Republic
b Present address: Plant Cell Biology, University of Lund, S-22007 Lund, Sweden
c Institute of Hematology and Blood Transfusion, 101 03 Prague 10, Czech Republic
d Institute of Sera and Vaccines, 101 03 Prague 10, Czech Republic
e Present address: Selectide Corporation, Tucson, AZ 85737, U.S.A.
Abstract
Twenty amino acid residues peptides derived from the N-terminal domain of glycoprotein gp41 exhibit four different types of reactivity with human sera in the course of seroconversion. The differences in the accessibility of the peptide by immune apparatus can result from different binding of the knobs formed by trimers of glycoprotein gp120 to the surface of the viral particle. The region covered with peptides of higher immunoresponse may be involved in binding of knobs to the viral surface. The loss of knobs during ageing is probably the source of differences in the time-dependence of immunoresponse of different epitopes. Peptide fragments covering amino acids 580-588 and 592-612 have been already studied in detail from the point of view of their reactivity with sera and structure. Here we describe new reactive region between the residues 612-629. The structure features of corresponding peptide in solution (studied by 1H NMR spectroscopy) are different from those previously reported. In this particular case peptides corresponding to different regions of gp41 differ also in their structures in solution prior to the binding to the antibody.
