scholarly journals Nearest-neighbour analysis of myoglobin antigenic sites. Nearest-neighbour residues whose replacement can alter the environment of binding-site residue(s) and thus change their characteristics and binding capability

1980 ◽  
Vol 191 (3) ◽  
pp. 673-680 ◽  
Author(s):  
A L Kazim ◽  
M Z Atassi
Keyword(s):  
Binding Capacity ◽  
Antigenic Site ◽  
Sperm Whale ◽  
Antigenic Structure ◽  
Nearest Neighbour ◽  
X Ray ◽  
Antigenic Sites ◽  
Binding Capability ◽  
Sperm Whale Myoglobin ◽  
Neighbour Analysis

By using the known antigenic structure of sperm-whale myoglobin previously determined in this laboratory and the X-ray co-ordinates for the myoglobin molecule, we have calculated the nearest-atom distances between each of the residues of the antigenic sites and all the other amino acids of the myoglobin molecule. These calculations have enabled us to identify the nearest-neighbour residues to each of the residues in the five antigenic sites, and which thus describe the immediate molecular environment of the sites. The influences of chemical changes or replacements in these environmental residues on the binding capacity of an antigenic site, when considered together with replacements directly in the antigenic sites, are expected to account for the major effects and will be extremely useful in explaining the cross-reactions of myoglobins from various species. However, it is stressed that the analysis has limitations due to the qualitative estimates of the effects, the influences of substitutions of once-removed or even at more distant locations (especially when they are cumulative) and finally the influences of any conformational re-adjustments when these occur as a result of the replacement(s).

scholarly journals Distance calculation of residues neighbouring to lysozyme antigenic sites. Site-neighbouring residues whose evolutionary substitution can modify the characteristics and binding energy of the sites

1980 ◽  
Vol 187 (1) ◽  
pp. 163-172 ◽  
Author(s):  
M Z Atassi ◽  
A L Kazim
Keyword(s):  
Amino Acid ◽  
Binding Sites ◽  
Binding Capacity ◽  
Antigenic Structure ◽  
Amino Acid Substitutions ◽  
Protein Binding Sites ◽  
X Ray ◽  
Distance Calculation ◽  
Antigenic Sites ◽  
Nearest Neighbours

By using the antigenic structure of lysozyme determined in this laboratory and the X-ray co-ordinates we have calculated the closest-atom distances between each of the residues in the three antigenic sites and all the other amino acids of the lysozyme molecule. These calculations enabled us to identify the nearest neighbours to each of the site residues. Thus the immediate environment of each site residue is described. For the three antigenic sites there is a total of 71 neighbouring residues. The effects of evolutionary amino acid substitutions in site-neighbouring residues on the binding capacity of protein binding sites in general and on protein antigenic sites in particular are discussed. These, together with the direct replacements in site residues, will acount for the major effects. However, the limitations of this treatment are stressed. The smaller effects on antigenic sites of replacements at once-removed and even at more distant locations, which, when they become cumulative, could be considerable, are brought to attention, together with any influences of conformational readjustments that can take place as a result of evolutionary amino acid replacements.

scholarly journals Prediction and conformation by synthesis of two antigenic sites in human haemoglobin by extrapolation from the known antigenic structure of sperm-whale myoglobin

1977 ◽  
Vol 167 (1) ◽  
pp. 275-278 ◽  
Author(s):  
A L Kazim ◽  
M Z Atassi
Keyword(s):  
Sperm Whale ◽  
Antigenic Structure ◽  
Homologous Proteins ◽  
Human Haemoglobin ◽  
Antigenic Sites ◽  
Inductive Effects ◽  
Structural Analogy ◽  
Starting Model ◽  
Sperm Whale Myoglobin

The complete antigenic structure of sperm-whale myoglobin was previously determined in our laboratory. By structural analogy with myoglobin, two regions in human haemoglobin were predicted to comprise antigenic sites. One region was on the alpha-chain [alpha-(15-23)] and the other on the beta-chain [beta-(16-23)]. These two regions were synthesized, purified and characterized, and their immunochemistry was studied. Each peptide was able specifically to bind considerable amounts of haemoglobin antibodies. In a set of homologous proteins, barring any drastic conformational or electrostatic inductive effects exerted by the substitutions, and allowing for obstruction due to subunit interaction, the determination of the antigenic structure of one protein may serve as a useful starting model for the others.

scholarly journals The antibody response to myoglobin is independent of the immunized species. Analysis in terms of replacements in the antigenic sites and in environmental residues of the cross-reactions of fifteen myoglobins with sperm-whale myoglobin antisera raised in different species

1980 ◽  
Vol 191 (3) ◽  
pp. 681-697 ◽  
Author(s):  
S S Twining ◽  
H Lehmann ◽  
M Z Atassi
Keyword(s):  
Amino Acid ◽  
Antibody Response ◽  
Three Dimensional ◽  
Sperm Whale ◽  
Cross Reactivity ◽  
Antigenic Structure ◽  
Amino Acid Substitutions ◽  
Antigenic Sites ◽  
The Cross ◽  
Sperm Whale Myoglobin

The recent determination of the entire antigenic structure of sperm-whale myoglobin with rabbit and goat antisera has permitted the examination of whether the antigenic structure recognized by antibodies depends on the species in which the antisera are raised. Also, by knowledge of the antigenic structure, the molecular factors that determine and influence antigenicity can be better understood in terms of the effects of amino acid substitutions occurring in the antigenic sites and in the environmental residues of the sites. In the present work, the myoglobins from finback whale, killer whale, horse, chimpanzee, sheep, goat, bovine, echidna, viscacha, rabbit, dog, cape fox, mouse and chicken were examined for their ability to cross-react with antisera to sperm-whale myoglobin. By immunoadsorbent titration studies with radioiodinated antibodies, each of these myoglobins was able to bind antibodies to sperm-whale myoglobin raised in goat, rabbit, chicken, cat, pig and outbred mouse. It was found that the extent of cross-reaction of a given myoglobin was not dependent on the species in which the antisera were raised. This indicated that the antibody response to sperm-whale myoglobin (i.e. its antigenic structure) is independent of the species in which the antisera are raised and is not directed to regions of sequence differences between the injected myoglobin and the myoglobin of the immunized host. Indeed, in each antiserum from a given species examined, that antiserum reacted with the myoglobin of that species. The extent of this auto-reactivity for a given myoglobin was comparable with the general extent of cross-reactivity shown by that myoglobin with antisera raised in other species. The cross-reactivities and auto-reactivities (both of which are of similar extents for a given myoglobin) can be reasonably rationalized in terms of the effects of amino acid substitutions within the antigenic sites and within the residues close to these sites. These findings confirm that the antigenicity of the sites is inherent in their three-dimensional locations.

An Antigenic Site of Sperm Whale Myoglobin

Nature ◽  
1967 ◽  
Vol 215 (5096) ◽  
pp. 17-20 ◽  
Author(s):  
M. J. CRUMPTON
Keyword(s):  
Antigenic Site ◽  
Sperm Whale ◽  
Sperm Whale Myoglobin

X-ray crystal structure of the ferric sperm whale myoglobin: Imidazole complex at 2.0 Å resolution

1991 ◽  
Vol 217 (3) ◽  
pp. 409-412 ◽  
Author(s):  
Claudia Lionetti ◽  
Maria Grazia Guanziroli ◽  
Francesco Frigerio ◽  
Paolo Ascenzi ◽  
Martino Bolognesi
Keyword(s):  
Crystal Structure ◽  
Sperm Whale ◽  
X Ray ◽  
Sperm Whale Myoglobin

scholarly journals Cyanide Binding to Lucina pectinata Hemoglobin I and to Sperm Whale Myoglobin: An X-Ray Crystallographic Study

1999 ◽  
Vol 77 (2) ◽  
pp. 1093-1099 ◽  
Author(s):  
Martino Bolognesi ◽  
Camillo Rosano ◽  
Romeo Losso ◽  
Alberto Borassi ◽  
Menico Rizzi ◽  
...  
Keyword(s):  
Sperm Whale ◽  
X Ray ◽  
Lucina Pectinata ◽  
Crystallographic Study ◽  
Cyanide Binding ◽  
Sperm Whale Myoglobin

scholarly journals The reaction of ferric sperm whale myoglobin with imidazole: X-ray and binding study

1981 ◽  
Vol 37 (a1) ◽  
pp. C27-C27
Author(s):  
M. Bolognesi ◽  
E. Cannillo ◽  
P. Ascenzi ◽  
M. Brunori ◽  
G. M. Giacometti ◽  
...  
Keyword(s):  
Sperm Whale ◽  
Binding Study ◽  
X Ray ◽  
Sperm Whale Myoglobin

The antigenic structure of poliovirus

1989 ◽  
Vol 323 (1217) ◽  
pp. 467-478 ◽  
Keyword(s):  
Monoclonal Antibodies ◽  
Virus Particle ◽  
Structural Changes ◽  
Three Dimensional ◽  
Antigenic Structure ◽  
X Ray ◽  
Antigenic Sites ◽  
Type 3 ◽  
Insight Into

We have solved the structure of the Mahoney strain of type 1 and the Sabin (attenuated vaccine) strain of type 3 poliovirus by X -ray crystallographic methods. By providing a three-dimensional framework for the interpretation of a wealth of experimental data, the structures have yielded insight into the architecture and assembly of the virus particle, have provided information regarding the entry of virus into susceptible cells, and defined the sites on the virus particle that are recognized by neutralizing monoclonal antibodies. Thus locating mutations in variants selected for resistance to neutralizing monoclonal antibodies has defined three antigenic sites of the surface of the virion, and provided clues as to the mechanisms by which viruses escape neutralization. Finally, comparison of the structures of the two strains, together with analysis of sequences of many poliovirus strains, have begun to define the structural changes associated with serotypic differences between polioviruses.

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