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α1-Antichymotrypsin Inactivates Staphylococcal Cysteine Protease in Cross-Class Inhibition

α1-Antichymotrypsin Inactivates Staphylococcal Cysteine Protease in Cross-Class Inhibition

Benedykt Wladyka, Agata J Kozik, Michal Bukowski, Anna Rojowska, Tomasz Kantyka, Grzegorz Dubin, Adam Dubin

Biochimie. 2011 May;93(5):948-53.

PMID: 21296644

Abstract:

Staphylococcal cysteine proteases are implicated as virulence factors in human and avian infections. Human strains of Staphylococcus aureus secrete two cysteine proteases (staphopains A and B), whereas avian strains express staphopain C (ScpA2), which is distinct from both human homologues. Here, we describe probable reasons why the horizontal transfer of a plasmid encoding staphopain C between avian and human strains has never been observed. The human plasma serine protease inhibitor α(1)-antichymotrypsin (ACHT) inhibits ScpA2. Together with the lack of ScpA2 inhibition by chicken plasma, these data may explain the exclusively avian occurrence of ScpA2. We also clarify the mechanistic details of this unusual cross-class inhibition. Analysis of mutated ACHT variants revealed that the cleavage of the Leu383-Ser384 peptide bond results in ScpA2 inhibition, whereas hydrolysis of the preceding peptide bond leads to ACHT inactivation. This evidence is consistent with the suicide-substrate-like mechanism of inhibition.

Chemicals Related in the Paper:

Catalog Number	Product Name	Structure	CAS Number	Price
AP141176923	α1-Antichymotrypsin from human plasma		141176-92-3	Price

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