Identification of a family of Bsp-A like surface proteins of Entamoeba histolytica with novel leucine rich repeats.

Authors

Paul H. Davis, University of Nebraska at OmahaFollow
Zhi Zhang, Washington University School of Medicine
Minghe Chen, Washington University School of Medicine in St. Louis
Xiaochun Zhang, Washington University School of Medicine in St. Louis
Subhra Chakraborty, Washington University School of Medicine
Samuel L. Stanley Jr., Washington University School of Medicine

Document Type

Article

Publication Date

1-2006

Publication Title

Mol Biochem Parasitol

Volume

145

Issue

1

First Page

111

Last Page

116

Abstract

Leucine rich repeats serve as recognition motifs for surface proteins from bacteria and eukaryotes. The BspA protein from Bacteroides forsythus mediates bacterial binding to fibronectin and contains leucine rich repeats of the Treponema pallidum (TpLRRP) family. Here we show that the protozoan parasite Entamoeba histolytica contains multiple BspA-like proteins, including a family of surface proteins which possess a new form of a leucine rich repeat that differs from the standard Treponema pallidum- like leucine rich repeat (TpLRRP) by possessing two conserved cysteine residues.

Comments

Published in final edited form as: Mol Biochem Parasitol. 2006 January ; 145(1): 111–116.

https://doi.org/10.1016/j.molbiopara.2005.08.017

Recommended Citation

Davis, Paul H.; Zhang, Zhi; Chen, Minghe; Zhang, Xiaochun; Chakraborty, Subhra; and Stanley, Samuel L. Jr., "Identification of a family of Bsp-A like surface proteins of Entamoeba histolytica with novel leucine rich repeats." (2006). Biology Faculty Publications. 118.
https://digitalcommons.unomaha.edu/biofacpub/118

Creative Commons License

This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 4.0 License.