scholarly journals Identification of Immunodominant CD4-Restricted Epitopes Co-Located with Antibody Binding Sites in Individuals Vaccinated with ALVAC-HIV and AIDSVAX B/E

PLoS ONE ◽  
2015 ◽  
Vol 10 (2) ◽  
pp. e0115582 ◽  
Author(s):  
Silvia Ratto-Kim ◽  
Mark S. de Souza ◽  
Jeffrey R. Currier ◽  
Nicos Karasavvas ◽  
John Sidney ◽  
...  
1993 ◽  
Vol 2 (2) ◽  
pp. 175-182 ◽  
Author(s):  
Christian Schwab ◽  
Andrea Twardek ◽  
Hans Rudolf Bosshard ◽  
Terence P. Lo ◽  
Gary D. Brayer

Microbiology ◽  
1987 ◽  
Vol 133 (4) ◽  
pp. 825-833 ◽  
Author(s):  
I. J. Nicolson ◽  
A. C. F. Perry ◽  
M. Virji ◽  
J. E. Heckels ◽  
J. R. Saunders

1981 ◽  
Author(s):  
R M Lewis ◽  
H M Reisner ◽  
B C Abels ◽  
H R Roberts

Affinity chromatography of an inhibitor to human factor IX (F.IX) separated the antibody into two populations. The ion dependent population of antibodies had an absolute divalent cation (Me++) binding requirement. The non-ion dependent population bound F.IX equally in the presence or absence of Me++. The concentration of Me++ required for ½ the maximum ion dependent antibody binding (½ max) was (in nM) Ca++ 0.40, Mn++ 0.05, Sr++ 0.70 and Mg++ 0.65.Ca++ potentiated the binding of antibody in the presence of excess Mg++. In addition, the ½ max for Ca++ was reduced about four fold. These observations are consistent with separate binding sites on the F.IX molecule for Ca++ and Mg++ and potentiation of Ca++ binding by Mg++. Scat- chard analysis of ion dependent antibody binding indicates about a 10 fold greater affinity of antibody in the presence of Ca++ than Mg++. In the presence of both cations, affinity was at least as high as in the presence of Ca++ alone supporting the presence of separate ion binding sites on the F.IX molecule.


1971 ◽  
Vol 133 (3) ◽  
pp. 589-601 ◽  
Author(s):  
Julia M. Phillips-Quagliata ◽  
Bernard B. Levine ◽  
Franco Quagliata ◽  
Jonathan W. Uhr

The mechanism of binding of immune complexes to macrophages was investigated using purified antibody and haptens of different valences. Antibody alone bound to macrophages; enhancement of binding occurred when polyvalent and divalent haptens were present at equivalence but did not occur in great antigen excess. Monovalent hapten did not increase the binding of antibody at any concentration ratio tried, though it inhibited the enhancement due to oligovalent hapten. Ultracentrifuged normal rabbit globulin also inhibited the binding of complexes indicating the presence of exposed binding sites on the uncomplexed molecules. Complexes bound more strongly than antibody alone as determined from elution studies. These results support the hypothesis that the enhancement of antibody binding to macrophages in the presence of antigen is due to increased energy of binding resulting from summation of individual binding sites already exposed on the antibody molecules. It was also possible, by saturating the macrophages with gamma globulin, to estimate the number of binding sites per cell; this was calculated to be approximately 2 million per alveolar macrophage.


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