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A murine monoclonal antibody, which binds to an epitope on the major outer membrane protein of Chlamydia trachomatis and with species specificity in the micro-immunofluorescent assay, effectively neutralized in vitro two antigenically distinct serovars of C. trachomatis. Optimal concentrations of both organism and antibody were required to produce maximal neutralization of the organism. Neutralization was less effective and more variable at lower dilutions of antibody than at higher dilutions, suggesting a prozone phenomenon. A radiolabeled attachment assay demonstrated that attachment of elementary bodies was unaffected by earlier treatment with antibody and that neutralization occurred at a step after attachment. The epitope to which this antibody is directed, on the major outer membrane protein of C. trachomatis, may have an important role in determining infectivity of the organism.
R Peeling, and
I W Maclean, and
R C Brunham
May 1994,
Infection and immunity,
R Peeling, and
I W Maclean, and
R C Brunham
August 1991,
Infection and immunity,
R Peeling, and
I W Maclean, and
R C Brunham
November 1982,
Infection and immunity,
R Peeling, and
I W Maclean, and
R C Brunham
August 2001,
Current opinion in immunology,
R Peeling, and
I W Maclean, and
R C Brunham
October 1993,
Infection and immunity,
R Peeling, and
I W Maclean, and
R C Brunham
January 1997,
Infection and immunity,
R Peeling, and
I W Maclean, and
R C Brunham
January 1987,
Journal of immunology (Baltimore, Md. : 1950),
R Peeling, and
I W Maclean, and
R C Brunham
September 1986,
Infection and immunity,
R Peeling, and
I W Maclean, and
R C Brunham
December 1995,
Zhongguo yi xue ke xue yuan xue bao. Acta Academiae Medicinae Sinicae,
R Peeling, and
I W Maclean, and
R C Brunham
April 1991,
Veterinary microbiology,
