Correlation between segmental mobility and the location of antigenic determinants in proteins

Abstract

Most continuous antigenic determinants of tobacco mosaic virus protein (TMVP), myoglobin and lysozyme correspond to those surface regions in the protein structure, as determined by X-ray crystallography, which possess a run of high-temperature factors along the polypeptide backbone, that is, a high segmental mobility. The mobility of an antigenic determinant may make it easier to adjust to a pre-existing antibody site not fashioned to fit the exact geometry of a protein. The correlation found between temperature factors and antigenicity is better than that between hydrophilicity and antigenicity.

Antibodies against synthetic amphipathic helical sequences of surfactant protein SP‐B detect a conformational change in the native protein

“…In con. trast, the antisera developed against the N-terminal sequence of SP-B only react with the native monomers in the reduced state suggesting that this domain has under|one ¢ontormational chan¢e~ after disulfide bond formation and oli$omerization, These results su88est that C-terminal sesments of native SP-B are less constrained hence more mobile than other sections or the polypeptide chain, and are surface.oriented as is typical or C-terminal domains in many proteins [17,18].…”

α‐MSH and neurofilament M‐protein share a continuous epitope but not extended sequences

“…In addition, a rabbit antiserum known to recognize the amino-terminal 10 residues of coat protein [13] recognizes M-protein on Western blots, although very weakly (not shown).…”

“…The amino-terminal region of TMV coat protein belongs to the increasing list of linear or continuous epitopes thought to be prime antigenic targets because of their segmental mobility as revealed by X-ray crystallography [ 13,161. Such sites are very often situated in loops and can also occur at the termini of different proteins [ 11,13,16].…”

“…Such sites are very often situated in loops and can also occur at the termini of different proteins [ 11,13,16]. Current concepts of intermediate filament structure based on biochemical and sequence considerations already suggest the presence of loops in the amino-terminal region of M-protein as in other intermediate filament proteins [9, lo].…”

A key amino acid determining G3m(b) allotypic markers

“…They are based on various guidances, such as segmental mobility (Westhof et aL, 1984), hydrophilicity (Hopp, 1986), large probe accessibility (Novotny et al, 1987), high local mobility, convex surface shape, or negative electrostatic potential (Geysen etk al., 1987). In brief, the epitopes of protein are determined by residues of the sites with a high accessibility of water molecule.…”