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• W2600696041 endingPage "e12741" @default.
• W2600696041 startingPage "e12741" @default.
• W2600696041 abstract "Blastomycosis elicits a pyogranulomatous inflammatory response that involves a prominent recruitment of neutrophils to the site of infection. Although neutrophils are efficiently recruited to the site of infection, this event is paradoxically coupled with the host's inability to control infection by Blastomyces dermatitidis, the causative agent. The mechanisms underlying this characteristic pyogranulomatous response and inability of neutrophils to kill the yeast are poorly understood. We recently reported that the fungal protease dipeptidyl peptidase IVA (DppIVA) promotes B. dermatitidis virulence by cleaving a dipeptide from the N-terminus of C-C chemokines and granulocyte/macrophage-colony stimulating factor, thereby inactivating them. Herein, we present evidence that DppIVA can also truncate the N-terminus of members of the ELR+ CXC chemokine family, which are known to modulate neutrophil function. We show that the DppIVA cleaved form of human (h) CXCL-2, for example, hCXCL-2 (3-73), is a more potent neutrophil chemoattractant than its intact counterpart, but hCXCL-2 (3-73) is conversely impaired in its ability to prime the reactive oxygen species response of neutrophils. Thus, DppIVA action on ELR+ CXC chemokines may promote the pyogranulomatous response that is typical of blastomycosis, while also explaining the inability of neutrophils to control infection." @default.
• W2600696041 created "2017-04-07" @default.
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• W2600696041 date "2017-05-30" @default.
• W2600696041 modified "2023-09-26" @default.
• W2600696041 title "<i>Blastomyces dermatitidis</i>serine protease dipeptidyl peptidase IVA (DppIVA) cleaves ELR⁺CXC chemokines altering their effects on neutrophils" @default.
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• W2600696041 doi "https://doi.org/10.1111/cmi.12741" @default.
• W2600696041 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5544578" @default.
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• W2600696041 hasPublicationYear "2017" @default.
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