Crystal structure of theStreptococcus agalactiaeCAMP factor, and insights into its membrane-permeabilizing activity

Journal: Journal of Biological Chemistry

Published: 2018-06-08

DOI: 10.1074/jbc.ra118.002336

Affiliations: 6

Authors: 7

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Research Highlight

Toxin from group B streptococcus decoded

© Rodolfo Parulan Jr./Getty

© Rodolfo Parulan Jr./Getty

Researchers have elucidated the structure of the bacterial protein used to diagnose group B streptococcal infections, and this has helped clarify the mechanism by which the toxic protein perforates and destroys red blood cells.

The ‘CAMP test’ used to identify group B streptococcal infections relies on the fact that the blood-bursting ability of an unrelated bacterium is enhanced in the presence the pore-forming toxin CAMP factor from Streptococcus agalactiae, the bug responsible for group B strep.

Now, a team co-led by investigators from the University of Science and Technology of China has determined the atomic structure of the CAMP factor. This has revealed the section of the protein involved in making cell membranes permeable and the region needed for promoting the breakdown of blood cells.

The findings could lead to new diagnostic tests and treatments for group B strep.

Supported content

  1. Journal of Biological Chemistry 293, 11867–11877 (2018). doi: 10.1074/jbc.RA118.002336
Institutions FC
Department of Chemistry, University of Waterloo, Canada 0.29
CAS Key Laboratory of Innate Immunity and Chronic Disease, USTC, China 0.21
Hefei National Laboratory for Physical Sciences at the Microscale (HFNL), China 0.21
Shanghai Sixth People's Hospital, SJTU, China 0.14
USDA-ARS Western Regional Research Center (WRRC), United States of America (USA) 0.07
USDA-ARS Healthy Processed Foods Research Unit (HPFR), United States of America (USA) 0.07

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