Abstract:
:Staphylococcus is a leading cause of microbial keratitis, characterized by destruction of the cornea by bacterial exoproteins and host-associated factors. The aim of this study was to compare extracellular and cell-associated proteins produced by two different isolates of S. aureus, a virulent clinical isolate (Staph 38) and a laboratory strain (Staphylococcus aureus 8325-4) of weaker virulence in the mouse keratitis model. Proteins were analyzed using 2D polyacrylamide gel electrophoresis and identified by subsequent mass spectrometry. Activity of staphylococcal adhesins was assessed by allowing strains to bind to various proteins adsorbed onto polymethylmethacrylate squares. Thirteen proteins in the extracellular fraction and eight proteins in the cell-associated fractions after bacterial growth were produced in increased amounts in the clinical isolate Staph 38. Four of these proteins were S. aureus virulence factor adhesins, fibronectin binding protein A, staphopain, glyceraldehyde-3-phosphate dehydrogenase 2 and extracellular adherence protein. The clinical isolate Staph 38 adhered to a greater extent to all mammalian proteins tested, indicating the potential of the adhesins to be active on its surface. Other proteins with increased expression in Staph 38 included potential moonlighting proteins and proteins involved in transcription or translation. This is the first demonstration of the proteome of S. aureus isolates from keratitis. These results indicate that the virulent clinical isolate produces more potentially important virulence factors compared to the less virulent laboratory strain and these may be associated with the ability of a S. aureus strain to cause more severe keratitis.
journal_name
Exp Eye Resjournal_title
Experimental eye researchauthors
Khan S,Cole N,Hume EB,Garthwaite LL,Nguyen-Khuong T,Walsh BJ,Willcox MDdoi
10.1016/j.exer.2016.08.016subject
Has Abstractpub_date
2016-10-01 00:00:00pages
171-8eissn
0014-4835issn
1096-0007pii
S0014-4835(16)30233-0journal_volume
151pub_type
杂志文章abstract::Polyclonal antisera have been made to synthetic peptides corresponding to the N- and C-terminal regions of the putative gamma 1-2 gene from human lens. These antisera are specific for gamma crystallin, showing no cross-reactivity with any polypeptides of the alpha- and beta-crystallin fractions. Western blot analysis ...
journal_title:Experimental eye research
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journal_title:Experimental eye research
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journal_title:Experimental eye research
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journal_title:Experimental eye research
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journal_title:Experimental eye research
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journal_title:Experimental eye research
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journal_title:Experimental eye research
pub_type: 杂志文章
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journal_title:Experimental eye research
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journal_title:Experimental eye research
pub_type: 杂志文章
doi:10.1016/j.exer.2006.07.020
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doi:10.1016/j.exer.2020.108292
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journal_title:Experimental eye research
pub_type: 杂志文章
doi:10.1016/s0014-4835(85)80017-8
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journal_title:Experimental eye research
pub_type: 杂志文章
doi:10.1006/exer.1994.1036
更新日期:1994-04-01 00:00:00
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pub_type: 杂志文章,评审
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journal_title:Experimental eye research
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doi:10.1016/j.exer.2007.08.020
更新日期:2007-12-01 00:00:00
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journal_title:Experimental eye research
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journal_title:Experimental eye research
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journal_title:Experimental eye research
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journal_title:Experimental eye research
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journal_title:Experimental eye research
pub_type: 杂志文章
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journal_title:Experimental eye research
pub_type: 杂志文章
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journal_title:Experimental eye research
pub_type: 杂志文章
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更新日期:2010-12-01 00:00:00
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journal_title:Experimental eye research
pub_type: 杂志文章
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