A Novel Peptide Can Mimic Extracellular Fibrinogen-Binding Protein to Block the Activation of Complement System

Extracellular fibrinogen-binding protein (Efb) of Staphylococcus aureus ( S. aureus ) is a bi-functional protein, which can specifically bind fibrinogen with its N terminus and inhibit deposition of C3b on the surface of S. aureus with its C terminus. Here, we screened the epitopes of Efb using phag...

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Bibliographic Details
Published in:Cell biochemistry and biophysics 2013-07, Vol.66 (3), p.753-757
Main Authors: Gao, Ya-ping, Dong, Jie, Zhang, Xin, Liu, Yu, Lu, Qiang, Feng, Jian-nan, Tan, Xiao-rong, Yang, Guang
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Bacterial Proteins - chemistry
Bacterial Proteins - metabolism
Biochemistry
Biological and Medical Physics
Biomedical and Life Sciences
Biophysics
Biotechnology
Cell Biology
Cell Death - drug effects
Complement Inactivator Proteins - chemistry
Complement Inactivator Proteins - metabolism
Complement System Proteins - metabolism
Erythrocytes - cytology
Erythrocytes - drug effects
Extracellular Space
Fibrinogen - metabolism
Humans
Life Sciences
Molecular Mimicry
Oligopeptides - chemistry
Oligopeptides - pharmacology
Original Paper
Peptides
Pharmacology/Toxicology
Staphylococcus aureus
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Summary:Extracellular fibrinogen-binding protein (Efb) of Staphylococcus aureus ( S. aureus ) is a bi-functional protein, which can specifically bind fibrinogen with its N terminus and inhibit deposition of C3b on the surface of S. aureus with its C terminus. Here, we screened the epitopes of Efb using phage display. Four peptides with consensus motif were screened. This consensus motif was identical to C terminus (161–164) of Efb. In the further investigation, it was found the synthesized peptide EC1 (154–165aa of Efb) could specifically bind C3/C3b and subsequently to block the activation of complement. Meanwhile, EC1 could inhibit the interaction between Efb and C3/C3b. Moreover, the interaction between the mutant protein of EmC1 (Efb without EC1) and C3 was decreased. And, the effect on the complement system of the mutant protein was dramatically declined compared with Efb. Our finding suggested that the peptide EC1 could mimic Efb to block complement system activation via binding C3.
ISSN:1085-9195
1559-0283
DOI:10.1007/s12013-013-9520-0