The structure of the OmpA/Pal protein of Anaplasma phagocytophilum
Cadby, I. T.
Show abstract
Peptidoglycan associated lipoprotein (Pal) and Outer Membrane Protein A (OmpA), interact with the outer membrane and peptidoglycan in Gram-negative bacteria, conferring structural integrity to the bacterial cell and functioning in cell division. Both OmpA and Pal proteins have moonlighting roles as virulence factors, facilitating infection and host-pathogen interactions in a range of bacteria. The OmpA-like protein of Anaplasma phagocytophilum, a tick-borne pathogen that infects a wide range of hosts, seems to function primarily as a virulence factor, since this bacterium lacks a peptidoglycan cell wall. Here we present crystal structures of the OmpA-like protein of A. phagocytophilum, demonstrating that this protein has amino acid insertions that confer flexibility. This insertion is also found in the OmpA-like proteins of other pathogens, related to A. phagocytophilum. Whether this flexibility is reflective of any adaptations for host-pathogen interactions remains to be determined but, since the OmpA-like proteins of Anaplasma species are current targets for vaccine development, might have importance for these efforts.
Matching journals
The top 10 journals account for 50% of the predicted probability mass.
Similar papers in this journal
- BonA from Acinetobacter baumannii forms a divisome-localized decamer that supports outer envelope function 94%
- Peptidoglycan DD-peptidases have distinct activities that impact fitness of Acinetobacter baumannii 92%
- A Vibrio cholerae BolA-like protein is required for proper cell shape and cell envelope integrity 92%
Similar papers in this journal
- Bacterial hemophilin homologs and their specific type eleven secretor proteins have conserved roles in heme capture and are diversifying as a family 93%
- In silico discovery of the myxosortases that process MYXO-CTERM and three novel prokaryotic C-terminal protein-sorting signals that share invariant Cys residues 92%
- Serotype specific sugars impact structure but not functions of the trimeric autotransporter adhesin EmaA of Aggregatibacter actinomycetemcomitans. 92%
Similar papers in this journal
Similar papers in this journal
- Discovery and CryoEM Structure of FPM13, a Periplasmic Metalloprotein Unique to Francisella 93%
- Enterococcal cell wall remodelling underpins pathogenesis via the release of the Enteroccocal Polysaccharide Antigen (EPA) 93%
- A novel sialic acid-binding adhesin present in multiple species contributes to the pathogenesis of infective endocarditis 93%
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.