Correlating low-similarity peptide sequences and HIV B-cell epitopes.
Although a large number of human immunodeficiency virus-1 (HIV-1) derived B-cell epitopes has been experimentally identified, the structural requirements underlying HIV humoral immune response remain unknown. Here, we review the current literature on HIV B-cell epitopes as catalogued in the www.hiv.lanl.gov/content/immunology website, searching for common structural and/or functional immunogenic motifs. The analysis of HIV antibody data documents that the linear determinants recognized by human or murine humoral immune responses, are (or harbor) pentapeptide fragments with no or only very low similarity to the respective host proteome. The present literature analysis provides relevant insights that may be applied to design anti-HCV therapeutic approaches exempt from autoimmune collateral effects.
Kanduc
Darja
D
Department of Biochemistry and Molecular Biology Ernesto Quagliariello, University of Bari, Italy. d.kanduc@biologia.uniba.it
Serpico
Rosario
R
Lucchese
Alberta
A
Shoenfeld
Yehuda
Y
D000595:Amino Acid Sequence; D000818:Animals; D000917:Antibody Formation; D018985:Epitopes, B-Lymphocyte / Q000737:chemistry / Q000276:immunology*; D015483:HIV Antibodies / Q000276:immunology*; D015488:HIV Antigens / Q000737:chemistry / Q000276:immunology*; D015658:HIV Infections / Q000276:immunology* / Q000821:virology; D015497:HIV-1 / Q000276:immunology*; D006801:Humans; D020543:Proteome / Q000276:immunology
D018985:Epitopes, B-Lymphocyte; D015483:HIV Antibodies; D015488:HIV Antigens; D020543:Proteome