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9B3H

Structure of a complex between Pasteurella multocida surface lipoprotein, PmSLP-1, and bovine complement factor I

Summary for 9B3H
Entry DOI10.2210/pdb9b3h/pdb
EMDB information44139
DescriptorComplement factor I, Pasteurella multocida factor I binding protein, fIbp, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (4 entities in total)
Functional Keywordsbacterial surface lipoprotein, complement protein, immune evasion, membrane protein
Biological sourcePasteurella multocida 36950
More
Total number of polymer chains2
Total formula weight103240.66
Authors
Nguyen, Q.H.,Norris, M.J.,Moraes, T.F. (deposition date: 2024-03-19, release date: 2025-04-23, Last modification date: 2025-06-04)
Primary citationNguyen, Q.H.,Lai, C.H.R.,Norris, M.J.,Ng, D.,Shah, M.,Lai, C.C.,Isenman, D.E.,Moraes, T.F.
A surface lipoprotein on Pasteurella multocida binds complement factor I to promote immune evasion.
Plos Pathog., 21:e1012686-e1012686, 2025
Cited by
PubMed Abstract: Pasteurella multocida is the leading cause of wound infections in humans following animals' bites or scratches. This bacterium is also commonly found in the respiratory tract of many mammals and can cause serious diseases resulting in the rapid death of infected animals, especially cattle. To prevent these infections in cattle, a subunit-based vaccine utilizing the surface lipoprotein PmSLP was developed and showed remarkable protection with a single dose administration. Here, we report that PmSLP binds host complement factor I (FI) and facilitates cleavage of complement components C3b and C4b independently of any cofactors (e.g., FH, C4BP), thereby allowing the pathogen to evade host defence. Cryo-EM structure of PmSLP bound to FI reveals that PmSLP stimulates FI enzymatic activity by stabilizing the catalytic domain. This is the first time that a bacterial protein has been shown to directly activate FI independent of complement cofactors and target all arms of the complement cascade.
PubMed: 40327719
DOI: 10.1371/journal.ppat.1012686
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4 Å)
Structure validation

237735

건을2025-06-18부터공개중

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