Journal
ARCHIVES OF MICROBIOLOGY
Volume 203, Issue 5, Pages 2563-2573Publisher
SPRINGER
DOI: 10.1007/s00203-021-02255-0
Keywords
Heparin; SpA; S; aureus; Infection
Categories
Funding
- National Natural Science Foundation of China [31670120]
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The study revealed that the protein A (SpA) of Staphylococcus aureus is a heparin-binding protein, contributing to the interaction between S. aureus and heparin. Mutating SpA or deleting the spa gene can reduce the binding capability of S. aureus to heparin.
Heparin, known for its anticoagulant activity, is commonly used as the coatings of medical devices. The attaching of Staphylococcus aureus, a prominent human and animal pathogen, to the heparin coatings usually leads to catheter-related bloodstream infections. Hence, the study of the interaction between heparin and S. aureus surface proteins is desired. Here, we found that protein A (SpA) of S. aureus was a heparin-binding protein, contributing to the interaction between S. aureus and heparin. The cell-wall-anchored SpA was one of the most critical S. aureus virulence factors with a lysin-like motif (LysM). When SpA was mutated to remove the LysM motif, the heparin-binding capability of SpA dropped 50%. The in-frame deletion of spa also reduced the heparin-binding capability of S. aureus. There was 1.3-fold more of heparin bound to wild type S. aureus than the Delta spa::Em strain. These results would help understand the host-microbe interaction and the infection by S. aureus.
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