Structure of the UspA1 protein fragment from Moraxella catarrhalis responsible for C3d binding.

ABSTRACT: The gram-negative bacterium Moraxella catarrhalis infects humans exclusively, causing various respiratory tract diseases, including acute otitis media in children, septicaemia or meningitis in adults, and pneumonia in the elderly. To do so, M. catarrhalis expresses virulence factors facilitating its entry and survival in the host. Among them are the ubiquitous surface proteins (Usps): A1, A2, and A2H, which all belong to the trimeric autotransporter adhesin family. They bind extracellular matrix molecules and inhibit the classical and alternative pathways of the complement cascade by recruiting complement regulators C3d and C4b binding protein. Here, we report the 2.5 Å resolution X-ray structure of UspA1^299-452, which previous work had suggested contained the canonical C3d bind

SUBMITTER: Mikula KM 

PROVIDER: S-EPMC6839023 | biostudies-literature | 2019 Nov

REPOSITORIES: biostudies-literature