A Monoclonal Antibody Directed Against the 97-kilodalton Gonococcal Hemin-binding Protein Inhibits Hemin Utilization by Neisseria Gonorrhoeae

Overview

Journal Infect Immun

Publisher American Society for Microbiology

Specialty Allergy & Immunology

Date 1997 Jul 1

PMID 9199474

Citations 6

Authors

B C Lee

S Levesque

Affiliations

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Abstract

Neisseria gonorrhoeae expresses two hemin-binding proteins (HmBPs) of 97,000 and 44,000 in molecular weight. A murine monoclonal antibody (MAb) produced against the 97-kDa HmBP from N. gonorrhoeae PID543 specifically inhibited in a concentration-dependent manner the ability of hemin to promote growth. The anti-97-kDa HmBP MAb competitively inhibited binding of the 97-kDa HmBP to a hemin-agarose affinity column. In Western immunoblots, the MAb recognized the 97-kDa homologs from a limited survey of clinical gonococcal isolates. These results support the contention that the 97-kDa HmBP is involved in the gonococcal hemin acquisition pathway.

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