This paper analyzes the HIV-1 gp120 epitope specificity and activation mechanisms (i.e., polyclonal versus oligoclonal) of antibodies present in the sera of alloimmune mice and humans. Sera from CBA mice engrafted with C57BL/6 lymphoid cells significantly reacted against the gp120-derived peptide aa 261-270, which shares high homology with the membrane-proximal domain of HLA class II beta-chains (HLA/gp120) and against the HIV gp120 V3 loop-derived peptides DP32 (HIV-1 MN-derived aa 302-334) and C53 (HIV-1 IIIB-derived aa 304-318). The same sera also reacted against the HIV-unrelated peptide necdin. Moreover, sera from BALB/c mice injected with LPS presented antibodies reacting against both HIV-related and -unrelated peptides, suggesting that similar mechanisms are shared in alloimmune and LPS-treated mice. A similar analysis was then performed on the sera of patients affected with beta-thalassemia major, receiving at least 10 blood transfusions/year. In particular, 15 of 58 (26%) sera from HIV-uninfected thalassemic patients showed a significantly reactivity against the HLA/gp120-derived peptides. Moreover, 22 of 58 (38%) sera from the same cohort showed a significant reactivity against DP32 peptide. This reactivity was related to a polyclonal activation mechanism since the DP32-reactive sera significantly bound a panel of HIV-unrelated peptides, as observed by testing 22 sera against necdin, 21 against HSP65 kDa, 21 against amyloid-1, and 17 against MAGE-1 peptides. Moreover, a significant increase of IgG concentration was also observed in all thalassemic sera, when compared to healthy controls, without regard to the anti-gp120 antibody reactivity. Taken together, these results indicate that (i) allogeneic stimuli may induce anti-gp120 antibodies in CBA and in 38% of polytransfused patients and (ii) this reactivity is related to a polyclonal activation mechanism but not to a heightened concentration of IgG. (C) 1997 Academic Press.

Fraziano, M., Montesano, C., Lombardi, V., Marchione, O.P., & Colizzi, V. (1997). The presence of antibodies against HIV peptides in the sera of alloimmune mice and thalassemic patients is due to a polyclonal activation mechanism. CLINICAL IMMUNOLOGY AND IMMUNOPATHOLOGY, 84(2), 202-207 [10.1006/clin.1997.4394].

The presence of antibodies against HIV peptides in the sera of alloimmune mice and thalassemic patients is due to a polyclonal activation mechanism

FRAZIANO, MAURIZIO;Montesano, C;COLIZZI, VITTORIO
1997

Abstract

This paper analyzes the HIV-1 gp120 epitope specificity and activation mechanisms (i.e., polyclonal versus oligoclonal) of antibodies present in the sera of alloimmune mice and humans. Sera from CBA mice engrafted with C57BL/6 lymphoid cells significantly reacted against the gp120-derived peptide aa 261-270, which shares high homology with the membrane-proximal domain of HLA class II beta-chains (HLA/gp120) and against the HIV gp120 V3 loop-derived peptides DP32 (HIV-1 MN-derived aa 302-334) and C53 (HIV-1 IIIB-derived aa 304-318). The same sera also reacted against the HIV-unrelated peptide necdin. Moreover, sera from BALB/c mice injected with LPS presented antibodies reacting against both HIV-related and -unrelated peptides, suggesting that similar mechanisms are shared in alloimmune and LPS-treated mice. A similar analysis was then performed on the sera of patients affected with beta-thalassemia major, receiving at least 10 blood transfusions/year. In particular, 15 of 58 (26%) sera from HIV-uninfected thalassemic patients showed a significantly reactivity against the HLA/gp120-derived peptides. Moreover, 22 of 58 (38%) sera from the same cohort showed a significant reactivity against DP32 peptide. This reactivity was related to a polyclonal activation mechanism since the DP32-reactive sera significantly bound a panel of HIV-unrelated peptides, as observed by testing 22 sera against necdin, 21 against HSP65 kDa, 21 against amyloid-1, and 17 against MAGE-1 peptides. Moreover, a significant increase of IgG concentration was also observed in all thalassemic sera, when compared to healthy controls, without regard to the anti-gp120 antibody reactivity. Taken together, these results indicate that (i) allogeneic stimuli may induce anti-gp120 antibodies in CBA and in 38% of polytransfused patients and (ii) this reactivity is related to a polyclonal activation mechanism but not to a heightened concentration of IgG. (C) 1997 Academic Press.
Pubblicato
Rilevanza internazionale
Articolo
Sì, ma tipo non specificato
Settore MED/04 - Patologia Generale
English
Con Impact Factor ISI
IMMUNODEFICIENCY-VIRUS TYPE-1; 2ND CONSERVED DOMAIN; ENVELOPE PROTEIN; GP120; EPITOPE; AIDS; NEUTRALIZATION; PATHOGENESIS; SIMILARITY; MOLECULES
Fraziano, M., Montesano, C., Lombardi, V., Marchione, O.P., & Colizzi, V. (1997). The presence of antibodies against HIV peptides in the sera of alloimmune mice and thalassemic patients is due to a polyclonal activation mechanism. CLINICAL IMMUNOLOGY AND IMMUNOPATHOLOGY, 84(2), 202-207 [10.1006/clin.1997.4394].
Fraziano, M; Montesano, C; Lombardi, V; Marchione, O; Colizzi, V
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/2108/43531
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