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Article: Data on biological chemistry detailed by researchers at University of Michigan, Medical Department.
- Article from:
- Chemicals & Chemistry
- Article date:
- November 20, 2009
CopyrightCOPYRIGHT 2009 NewsRX. This material is published under license from the publisher through the Gale Group, Farmington Hills, Michigan. All inquiries regarding rights should be directed to the Gale Group. (Hide copyright information)
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"The protozoan parasite Toxoplasma gondii relies on posttranslational modification, including proteolysis, of proteins required for recognition and invasion of host cells. We have characterized the T. gondii cysteine protease cathepsin L (TgCPL), one of five cathepsins found in the T. gondii genome," researchers in the United States report.
"We show that TgCPL is the primary target of the compound morpholinurea-leucyl-homophenyl-vinyl sulfone phenyl (LHVS), which was previously shown to inhibit parasite invasion by blocking the release of invasion proteins from microneme secretory organelles. As shown by fluorescently labeled LHVS and TgCPL-specific antibodies, ...
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