Crystal structure of the Streptococcus agalactiae CAMP factor provides insights into its membrane-permeabilizing activity.

ABSTRACT: Streptococcus agalactiae is an important human opportunistic pathogen that can cause serious health problems, particularly among newborns and older individuals. S. agalactiae contains the CAMP factor, a pore-forming toxin first identified in this bacterium. The CAMP reaction is based on the co-hemolytic activity of the CAMP factor and is commonly used to identify S. agalactiae in the clinic. Closely related proteins are present also in other Gram-positive pathogens. Although the CAMP toxin was discovered more than a half century ago, no structure from this toxin family has been reported, and the mechanism of action of this toxin remains unclear. Here, we report the first structure of this toxin family, revealing a structural fold composed of 5 + 3-helix bundles. Furthe

SUBMITTER: Jin T 

PROVIDER: S-EPMC6066297 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature