Vaccination with Phage-Displayed Antigenic Epitope

Author(s):  
Yicun Wang ◽  
Li Wang
Keyword(s):  
2011 ◽  
Vol 186 (7) ◽  
pp. 3831-3835 ◽  
Author(s):  
Enayat Nikoopour ◽  
Christian Sandrock ◽  
Katrina Huszarik ◽  
Olga Krougly ◽  
Edwin Lee-Chan ◽  
...  

2020 ◽  
Author(s):  
Daniel J. Goetschius ◽  
Samantha R. Hartmann ◽  
Lindsey J. Organtini ◽  
Heather Callaway ◽  
Kai Huang ◽  
...  

AbstractOverlap on the surface of parvovirus capsids between the antigenic epitope and the receptor binding site contributes to species jumping. Mab 14 strongly binds and neutralizes canine, but not feline parvovirus. The high resolution map of the canine parvovirus capsid complexed with Fab 14 was used to solve local structures of the Fab-bound and -unbound antigenic sites extracted from the same complex. The subsequent analysis includes a new method for using cryo EM to investigate complementarity of antibody binding.


1996 ◽  
Vol 40 (6) ◽  
pp. 455-458 ◽  
Author(s):  
Toshiyuki Masuzawa ◽  
Kazuhide Kaneda ◽  
Hiroyuki Suzuki ◽  
Jianhui Wang ◽  
Kazuto Yamada ◽  
...  

2020 ◽  
Vol 132 (46) ◽  
pp. 20710-20718
Author(s):  
Juntao Cai ◽  
Jing Hu ◽  
Chunjun Qin ◽  
Lingxin Li ◽  
Dacheng Shen ◽  
...  

2012 ◽  
Vol 80 (8) ◽  
pp. 2956-2962 ◽  
Author(s):  
Shin-ichi Yokota ◽  
Ken-ichi Amano ◽  
Chiaki Nishitani ◽  
Shigeru Ariki ◽  
Yoshio Kuroki ◽  
...  

ABSTRACTWe propose two antigenic types ofHelicobacter pylorilipopolysaccharides (LPS): highly antigenic epitope-carrying LPS (HA-LPS) and weakly antigenic epitope-carrying LPS (WA-LPS) based on human serum reactivity. Strains carrying WA-LPS are highly prevalent in isolates from gastric cancer patients. WA-LPS exhibits more potent biological activities compared to HA-LPS, namely, upregulation of Toll-like receptor 4 (TLR4) expression and induction of enhanced epithelial cell proliferation. The results of competitive binding assays using monosaccharides and methylglycosides, as well as binding assays using glycosidase-treated LPS, suggested that β-linkedN-acetyl-d-glucosamine and β-linkedd-galactose residues largely contributed to the highly antigenic epitope and the weakly antigenic epitope, respectively. WA-LPS exhibited greater binding activity to surfactant protein D (SP-D) in a Ca2+-dependent manner, and this interaction was inhibited by methyl-β-d-galactoside. The biological activities of WA-LPS were markedly enhanced by the addition of SP-D. Lines of evidence suggested that removal of β-N-acetyl-d-glucosamine residue, which comprises the highly antigenic epitope, results in exposure of the weakly antigenic epitope. The weakly antigenic epitope interacted preferentially with SP-D, and SP-D enhanced the biological activity of WA-LPS.


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