scholarly journals Screening and Identification of a Chicken Dendritic Cell Binding Peptide by Using a Phage Display Library

2019 ◽  
Vol 10 ◽  
Author(s):  
Sunting Ma ◽  
Xinyuan Qiao ◽  
Yigang Xu ◽  
Li Wang ◽  
Han Zhou ◽  
...  
1994 ◽  
Vol 124 (3) ◽  
pp. 373-380 ◽  
Author(s):  
E Koivunen ◽  
B Wang ◽  
E Ruoslahti

Our previous studies showed that the alpha 5 beta 1 integrin selects cysteine pair-containing RGD peptides from a phage display library based on a random hexapeptide. We have therefore searched for more selective peptides for this integrin using a larger phage display library, where heptapeptides are flanked by cysteine residues, thus making the inserts potentially cyclic. Most of the phage sequences that bound to alpha 5 beta 1 (69 of 125) contained the RGD motif. Some of the heptapeptides contained an NGR motif. As the NGR sequence occurs in the cell-binding region of the fibronectin molecule, this sequence could contribute to the specific recognition of fibronectin by alpha 5 beta 1. Selection for high affinity peptides for alpha 5 beta 1 surprisingly yielded a sequence RRETAWA that does not bear obvious resemblance to known integrin ligand sequences. The synthetic cyclic peptide GACRRETAWACGA (*CRRETAWAC*) was a potent inhibitor of alpha 5 beta 1-mediated cell attachment to fibronectin. This peptide is nearly specific for the alpha 5 beta 1 integrin, because much higher concentrations were needed to inhibit the alpha v beta 1 integrin, and there was no effect on alpha v beta 3- and alpha v beta 5-mediated cell attachment to vitronectin. The peptide also did not bind to the alpha IIb beta 3 integrin. *CRRETAWAC* appears to interact with the same or an overlapping binding site in alpha 5 beta 1 as RGD, because cell attachment to *CRRETAWAC* coated on plastic was divalent cation dependent and could be blocked by an RGD-containing peptide. These results reveal a novel binding specificity in the alpha 5 beta 1 integrin.


Author(s):  
Anja Ziegler ◽  
Judith Olzhausen ◽  
Eman Hamza ◽  
Ana Stojiljkovic ◽  
Michael H. Stoffel ◽  
...  

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Xu Qiang ◽  
Keyong Sun ◽  
Lijun Xing ◽  
Yifeng Xu ◽  
Hong Wang ◽  
...  

2007 ◽  
Vol 13 (20) ◽  
pp. 6049-6055 ◽  
Author(s):  
Ping Zhao ◽  
Tessa Grabinski ◽  
Chongfeng Gao ◽  
R. Scot Skinner ◽  
Troy Giambernardi ◽  
...  

2013 ◽  
Vol 319 (8) ◽  
pp. 1156-1164 ◽  
Author(s):  
Wenhui Wang ◽  
Xilei Chen ◽  
Tao Li ◽  
Yanmei Li ◽  
Ruixue Wang ◽  
...  

2012 ◽  
Vol 58 (7) ◽  
pp. 898-908 ◽  
Author(s):  
Yanhua Zeng ◽  
Liangzhuan Liu ◽  
Jun He ◽  
Yan Liu ◽  
Cuiming Zhu ◽  
...  

Mycoplasma genitalium adhesion protein (MgPa) is the major adhesion protein of M. genitalium, and its C-terminal domain (amino acid 1075–1444) is the most immunogenic region. However, the exact epitopes of the adhesion protein of M. genitalium are still unclear. We used the purified polyclonal antibody against the recombinant adhesion protein to screen the mimic epitopes of MgPa using a random 12-peptide phage display library. Immunoscreening via the phage display peptide library revealed that 3 motifs (P-S-A-A/V-X-R-F/W-E/S-L-S-P, A-K-I/L-T/Q-X-T-L-X-L, and K-S-L-S-R-X-D-X-I) may represent 3 different mimotopes of MgPa. Results of bioinformatics analysis by MIMOX demonstrated that the key consensus amino acid residues in the aligned mimotopes may be S, A, and F for cluster 1; A, K, I, T, and L for cluster 2; and K, S, L, R, D, and I for cluster 3. Three representative phages could recognize sera from M. genitalium-positive patients to varying degrees, whereas they could not recognize the sera from Mycoplasma pneumoniae -positive patients or the sera from healthy people. These findings will help to clarify the mimic epitopes of MgPa to facilitate diagnosis of the antigen and to understand the antigenic structure of MgPa.


Sign in / Sign up

Export Citation Format

Share Document