Scl1, the multifunctional adhesin of group A Streptococcus, selectively binds cellular fibronectin and laminin, and mediates pathogen internalization by human cells.

Scl1, the multifunctional adhesin of group A Streptococcus, selectively binds cellular fibronectin and laminin, and mediates pathogen internalization by human cells.
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DOI:
10.1111/j.1574-6968.2009.01864.x
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发表时间:
2010-02
影响因子:
2.1
通讯作者:
Lukomski S
Lukomski S
中科院分区:
生物学4区
文献类型:
--
作者:
Caswell CC;Oliver-Kozup H;Han R;Lukomska E;Lukomski S

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The streptococcal collagen-like protein-1, Scl1, is widely expressed by the wellrecognized human pathogen group A Streptococcus(GAS). Screening of human ligands for binding to recombinant Scl1 identified cellular fibronectin and laminin as binding partners. Both ligands interacted with the globular domain of Scl1, which is also able to bind the low-density lipoprotein. Native Scl1 mediated GAS adherence to ligand-coated glass cover slips and promoted GAS internalization into HEp-2 cells. This work identifies new ligands of the Scl1 protein that are known to be important in GAS pathogenesis and suggests a novel ligandswitching mechanism between blood and tissue environments, thereby facilitating host colonization and GAS dissemination.
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