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Abstract

Complement offers a first line of defence against infection through the opsonization of microbial pathogens, recruitment of professional phagocytes to the infection site and the coordination of inflammatory responses required for the resolution of infection. is a successful pathogen that has developed multiple mechanisms to thwart host immune responses. Understanding the precise strategies employed by to bypass host immunity will be paramount for the development of vaccines and or immunotherapies designed to prevent or limit infection. To gain a better insight into the specific immune evasion mechanisms used by we examined the pathogen’s interaction with the soluble complement inhibitor, C4b-binding protein (C4BP). Previous studies indicated that recruits C4BP using a specific cell-wall-anchored surface protein and that bound C4BP limits complement deposition on the staphylococcal surface. Using flow-cytometric-based bacterial-protein binding assays we observed no interaction between and C4BP. Moreover, we offer a precautionary warning that C4BP isolated from plasma can be co-purified with minute quantities of human IgG, which can distort binding analysis between and human-derived proteins. Combined our data indicates that recruitment of C4BP is not a complement evasion strategy employed by .

Funding
This study was supported by the:
  • European Society of Clinical Microbiology and Infectious Diseases
    • Principle Award Recipient: MaisemLaabei
  • Academy of Medical Sciences (Award SBF006\1023)
    • Principle Award Recipient: MaisemLaabei
  • This is an open-access article distributed under the terms of the Creative Commons Attribution License. This article was made open access via a Publish and Read agreement between the Microbiology Society and the corresponding author’s institution.
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/content/journal/micro/10.1099/mic.0.001391
2023-09-05
2025-03-22
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