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The Preliminary Study on a Functional Peptide of FnBPA Protein Mediating Staphylococcus Aureus Invasion

Author: WangChenHong
Tutor: ShaoNingSheng；LiShaoHua
School: PLA Military Academy of Medical Sciences
Course: Biochemistry and Molecular Biology
Keywords: Staphylococcus aureus FnBPA Attack Fibronectin Fn 293 cells Functional peptides
CLC: R378
Type: Master's thesis
Year: 2007
Downloads: 44
Quote: 0
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Abstract


Staphylococcus aureus (hereinafter referred to as Staphylococcus aureus ) is a gram-positive pathogens , can cause a variety of diseases . Past studies suggest that Staphylococcus aureus belonging extracellular parasites . However , recent studies suggest that S. aureus invasion of a variety of non - professional phagocytes the FnBP protein invasion of host cells is mediated Staphylococcus aureus surface protein . Studies suggest that FnBP protein mediated through fibronectin binding to bacteria and binding to cells , wherein the key bit FnBPA and fibronectin protein binding point is located in the domain of the protein D , to repeat the sequence as a unit , including three successive complete repeat sequence D1, D2, D3 and a truncated D 4 sequence . Due the the steric relationship , if FnBP merely repeats units combined with the Fn molecule will inevitably result in the reduction of the actual binding sites and D4 truncated sequences function of redundancy . To ensure maximum bioavailability and binding , we speculated FnBPA D domain of Fn binding sites may not be to repeat the sequence as a unit , some truncated repeat sequence or having a binding function , or a repeated sequence and the lower part of the combination to generate a new binding site . The purpose of this experiment is more than speculate preliminary validation . According to the literature , we have established experimental model of bacterial invasion 293 cells , and found this model Staphylococcus aureus effective invasion strain 04018 as the experimental strains . Method of using genetic engineering , cloning of 04,018 strains FnBPA protein D 1 District C side and D of District N-terminal peptide gene fragment , and expressed in E. coli the fusion protein of GST and the peptide (FnBPA-D1c/D2n) . ELISA experiments confirmed that the desired peptide in the fusion protein capable of binding to Fn, bacterial invasion to cells in experiments confirmed the target peptide of the fusion protein can be suppressed aureus invasion of 293 cells , 50% of the protein inhibitor is about 20μg/ml , equivalent to 2.5μg / ml peptide . Through the study of the subject , we find D structure of the domain in of Staphylococcus aureus FnBPA protein with fibronectin-binding sites prompt FnBPA protein or has smaller binding units , or the presence of the Fn binding the point, rather than a forecast of 3-4 , and provides the basis for the inhibition of Staphylococcus aureus invasion of cells .

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CLC: > Medicine, health > Basic Medical > Medical Microbiology ( pathogenic bacteriology,pathogenic microbiology ) > Pathogenic bacteria
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