5bob

Publication Abstract from PubMed

Fhb is a surface virulence protein from Streptococcus suis, which could aid bacterial evasion of host innate immune defense by recruiting complement regulator factor H to inactivate C3b deposited on bacterial surface in blood. Here we successfully expressed and purified the N terminal domain of Fhb (N-Fhb) and obtained crystals of the N-Fhb by sitting-drop vapor diffusion method with a resolution of 1.50 A. The crystals belong to space group C2 with unit cell parameters a = 127.1 A, b = 77.3 A, c = 131.6 A, alpha = 90 degrees , beta = 115.9 degrees , gamma = 90 degrees . The structure of N-Fhb was determined by SAD method and the core structure of N-Fhb is a beta sandwich. We speculated that binding of Fhb to human factor H may be mainly mediated by surface amino acids with negative charges.

Expression, purification, crystallization and structure determination of the N terminal domain of Fhb, a factor H binding protein from Streptococcus suis.,Zhang C, Yu Y, Yang M, Jiang Y Biochem Biophys Res Commun. 2015 Oct 23;466(3):413-7. doi:, 10.1016/j.bbrc.2015.09.040. Epub 2015 Sep 10. PMID:26365348^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.