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J. Biol. Chem., Vol. 276, Issue 45, 41913-41920, November 9, 2001
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From the Department of Biochemistry, Tulane University Health
Sciences Center, New Orleans, Louisiana 70112
The specificity and intensity of
CD4+ helper T-cell responses determine the
effectiveness of immune effector functions. Promiscuously immunodominant helper T-cell epitopes in the human immunodeficiency virus (HIV) envelope glycoprotein gp120 could be important in the
development of broadly protective immunity, but the underlying mechanisms of immunodominance and promiscuity remain poorly defined. In
this study, gp120 helper T-cell epitopes were systematically mapped in
CBA/J and BALB/c mice by restimulation assays using a set of
overlapping peptides spanning the entire sequence of the gp120 encoded
by HIV strain 89.6. The results were analyzed in the context of the HIV
gp120 structure determined by x-ray crystallography. One major finding
was that all of the promiscuously immunodominant gp120 sequences are
located in the outer domain. Further analyses indicated that
epitope immunogenicity in the outer domain correlates with structural
disorder in adjacent N-terminal segments, as indicated by
crystallographic B-factors or sequence divergence. In contrast, the
correlation was poor when the analysis encompassed the entire gp120
sequence or was restricted to only the inner domain. These findings
suggest that local disorder promotes the processing and presentation of
adjacent epitopes in the outer domain of gp120 and therefore reveal how
three-dimensional structure shapes the profile of helper T-cell epitope immunogenicity.
To whom correspondence should be addressed. Tel.:
504-586-3990; Fax: 504-584-2739; E-mail: landry@tulane.edu.
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