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Mechanistic role for α3β1/CD151 and the neutrophilic fungal response to β‐Glucan
Author(s) -
Johnson Courtney M,
Byrd Angel,
Reichner Jonathan
Publication year - 2012
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.26.1_supplement.276.4
Subject(s) - glucan , integrin , chemotaxis , fibronectin , effector , candida albicans , microbiology and biotechnology , receptor , biology , epitope , chemistry , extracellular matrix , immunology , biochemistry , antibody
Polymorphonuclear leukocytes (PMNs) mediate host defense against fungal pathogens, such as C. albicans, through CR3 recognition of the fungal PAMP β‐glucan. β‐glucan is known to increase adhesion, chemotaxis, respiratory burst in PMNs via CR3. Since the PMN response to mycotic infections occurs within afflicted tissues, cells encounter extracellular matrix components which may regulate cell effector functions. Indeed, we found homotypic aggregations of neutrophils exposed to fibronectin and β‐glucan; but not to either one alone. In studies to determine the integrin mediated mechanism of homotypic aggregation, we discovered a role for αMβ1 and the TMF, CD151, in the formation of aggregates. Use of a mAbs against α3β1 attenuated aggregate formation. Use of TS151R Ab against CD151 at its α3β1 binding epitope led to smaller aggregates. These findings suggest a novel role for α3β1, a prototypical laminin receptor, in fungal defense involving CR3. The hypothesis resulting from these findings is that there is an integrin cross talk pathway through which β‐glucan ligation at the lectin site of CR3 activates α3β1.