Abstract
Major autolysin (Atl) of Staphylococcus aureusis a cell surface associated peptidoglycan hydrolase with amidase and glucosaminidase domains. Atl enzymes (amidase and glucosaminidase) are known to participate in biofilm formation and also can bind with host matrices. Earlier studies demonstrated the binding of Atlwithfibronectin, thrombospondin 1, vitronectin and heat shock cognate protein Hsc70. Here, we have shown, Atl mediates attachment of S.aureus to heparin and gelatine as well. The atl mutant strain demonstrated around 2.5 fold decreased adherence with fibronectin, gelatin and heparin coated microtiter plates. The microscopic studies confirmed the reduced binding of atl mutant with them compared to its parental wild type and complemented mutant strains. Amidase and glucosaminidase were expressed as N-terminal histidine tagged proteins from Escherichia coli, purified and refolded. We found refolded amidase bind with fibronectin, gelatin and heparin; whereas refolded glucosaminidase binds with only fibronectin and heparin but not gelatin. These results reemphasize Atl as one of the crucial proteins from Staphylococcus that facilitate their binding with multiple host cellular components during colonization and infection.
Highlights
Bacterial infections is a global concern due to its associated morbidity and mortality [1]
Binding assays was carried out to evaluate the attachment of the wild type SA113, atl mutant and complement mutant (SA113pTXatl) strains to Fn, He and Gein 96 well plates
It was observed from absorbance values that atl mutant strain binds less to Fn, He and Ge compared to the wild type and complement mutant strain (Fig. 1)
Summary
Bacterial infections is a global concern due to its associated morbidity and mortality [1]. The first step in any bacterial infection is the contact between bacteria and the host. Bacteria interact with the host using their surface proteins and adhesins. This interaction facilitates bacterial attachment and colonization which is a requirement for their successful pathogenesis [2]. Bacterial host protein interaction allows the Gram negative bacteria to inject their effector proteins into the host. Shigella infection is caused by the effector proteins injected into the host after it interacts with the host [4]. M protein of Streptococcus pyogenes [5], laminin binding protein (hlp) of Mycobacterium leprae [6,7], adhesion intimin of Escherichia coli [8,9,10], InlA and InlB, internalins of Listeria monocytogenes [4] are few other examples of bacterial proteins involved in attachment to host proteins
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