Faculty Advisor

Adams, David S.

Abstract

Neisseria gonorrhoeae infects humans in part because of the binding to its surface protein porin (Por) molecules by the complement control protein (CCP) domains 6 and 18-20 of the human complement regulator, factor H (fH). FH activity is thereby localized to the surface of N. gonorrhoeae and results in inactivation of the alternative pathway of complement. This project investigated the Por/fH interaction by creating species-specific sequence changes in human and chimpanzee CCP 20s in cloned fH proteins, and used flow cytometry to determine the ability of the recombinant proteins to bind N. gonorrhoeae. The data indicated that arginine located at position 1203 in fH CCP 20, R1203, is critical for fH-binding to N. gonorrhoeae.

Publisher

Worcester Polytechnic Institute

Date Accepted

January 2009

Major

Biology and Biotechnology

Project Type

Major Qualifying Project

Accessibility

Unrestricted

Advisor Department

Biology and Biotechnology

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