scholarly journals Localization of Antibody-Binding Sites by Sequence Analysis of Cloned Pilin Genes from Neisseria Gonorrhoeae

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
Keyword(s):  
Sequence Analysis ◽  
Neisseria Gonorrhoeae ◽  
Binding Sites ◽  
Antibody Binding

Sequence analysis of a PM2-DNA anti-Z-IgG-binding region

1984 ◽  
Vol 4 (10) ◽  
pp. 885-895 ◽  
Author(s):  
F. D. Miller ◽  
R. J. Winkfein ◽  
J. B. Rattner ◽  
J. H. Van de Sande
Keyword(s):  
Gene Regulation ◽  
Sequence Analysis ◽  
Binding Sites ◽  
Antibody Binding ◽  
Binding Region ◽  
Protein Coding ◽  
Left Handed ◽  
Igg Binding ◽  
Purine Pyrimidine

An anti-Z-antibody-binding region between PM2-DNA map units 0.05 and 0.18, containing approx. 25% of the bound PM2 antibody molecules (1,2) has been sequenced. Analysis of this PM2 DNA sequence from map units 0.00 to 0.175 demonstrates that alternating purine/pyrimidine tracts capable of adopting the left-handed conformation are present within this antibody-binding region. Longer (GC)n-rich tracts are clustered together and comprise seven alternating purine/pyrimidine-rich areas (48%–84%) ranging from 19 to 142 nucleotides in length. The DNA located between these alternating purine/pyrimidine-rich areas exhibit a low level (0%–19%) of this sequence arrangement. There is a very strong correlation between the alternating purine/pyrimidine-rich areas and the anti-Z-DNA-IgG-binding sites. Nucleotides 1461–1583 of the PM2-DNA genome encode the bacteriophage capsid protein IV. One of the PM2 left-handed sites is located within this protein-coding sequence; a B-to-Z transition within this site may be involved in protein-IV gene regulation in vivo.

scholarly journals Mapping antibody binding sites on cytochrome c with synthetic peptides: Are results representative of the antigenic structure of proteins?

1993 ◽  
Vol 2 (2) ◽  
pp. 175-182 ◽  
Author(s):  
Christian Schwab ◽  
Andrea Twardek ◽  
Hans Rudolf Bosshard ◽  
Terence P. Lo ◽  
Gary D. Brayer
Keyword(s):  
Cytochrome C ◽  
Binding Sites ◽  
Synthetic Peptides ◽  
Antibody Binding ◽  
Antigenic Structure ◽  
Structure Of Proteins

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 ◽  
...  
Keyword(s):  
Binding Sites ◽  
Antibody Binding

scholarly journals Variation of gonococcal lipooligosaccharide structure is due to alterations in poly-G tracts in lgt genes encoding glycosyl transferases.

1996 ◽  
Vol 183 (1) ◽  
pp. 323-327 ◽  
Author(s):  
Q L Yang ◽  
E C Gotschlich
Keyword(s):  
Sequence Analysis ◽  
Neisseria Gonorrhoeae ◽  
Experimental Evidence ◽  
High Frequency ◽  
Genetic Mechanism ◽  
Frequency Variation ◽  
Alpha Chain ◽  
Glycosyl Transferases ◽  
Genes Encoding

The lipooligosaccharide (LOS) expressed by gonococci spontaneously varies its structure at high frequency, but the underlying genetic mechanism has not been described. We have previously reported that the genes encoding the glycosyl transferases responsible for the biosynthesis of the variable alpha chain of the LOS of Neisseria gonorrhoeae are located in a locus containing five genes, lgtA, lgtB, lgtC, lgtD, and lgtE. Sequence analysis showed that lgtA, lgtC, and lgtD contained poly-G tracts within the coding frames, leading to the hypothesis that shifts in the number of guanosine residues in the poly-G tracts might be responsible for the high frequency variation in structure of gonococcal LOS. We now provide experimental evidence confirming this hypothesis.

The Effect Of Metal Ions On Human Factor IX Antigenicity

1981 ◽  
Author(s):  
R M Lewis ◽  
H M Reisner ◽  
B C Abels ◽  
H R Roberts
Keyword(s):  
Divalent Cation ◽  
Binding Sites ◽  
Human Factor ◽  
Antibody Binding ◽  
Factor Ix ◽  
Ion Binding ◽  
Human Factor Ix ◽  
Excess Mg ◽  
Ion Binding Sites ◽  
Two Populations

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.

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