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., 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
1997-01-01

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.
1997
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., 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: https://hdl.handle.net/2108/43531
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