scholarly journals Completion of the analysis of the primary structure of the variable domain of a homogeneous rabbit antibody to type III pneumococcal polysaccharide

1974 ◽  
Vol 143 (3) ◽  
pp. 723-732 ◽  
Author(s):  
Jean-Claude Jaton
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Guinea Pig ◽  
Heavy Chain ◽  
Variable Region ◽  
Complete Sequence ◽  
Rabbit Antibody ◽  
Type Iii ◽  
Minor Variant ◽  
V Region

The amino acid sequence between residues 70 and 116 of the V (variable) region of the H (heavy) chain derived from rabbit antibody BS-5, specific for type III pneumococcal polysaccharide, was determined. The sequence of this section of the H chain which includes the hypervariable residues 94 to about 112 was unique, although minor variant sequences present in the H chain preparation would not have been detected by the techniques used in this work. Taken together with the known sequences of the N-terminal 69 residues of H chain BS-5 (Jaton & Braun, 1972) and of the V region of the light chain (Jaton, 1974b), the data establish the complete sequence of the V domain of a rabbit immunoglobulin G. The V region of H chain BS-5 is compared with the basic sequences of the three human V region subgroups known to date, with one mouse H chain, and with guinea-pig pooled H chains. Even though chains from guinea pig and mouse clearly belong to the subgroup III of variability (VHIII), rabbit H chain BS-5 (allotypic variant a1) appears more closely related to the subgroup VHII than to the subgroups VHIII or VHI. The homology between VL and VH regions of antibody BS-5 (28%) is not greater than that observed between the VH region of antibody BS-5 and the VL regions of different rabbit antibodies.

scholarly journals Amino acid sequence of the N-terminal 139 residues of light chain derived from a homogeneous rabbit antibody

1974 ◽  
Vol 141 (1) ◽  
pp. 1-13 ◽  
Author(s):  
Jean-Claude Jaton
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Light Chain ◽  
Peptide Bond ◽  
Complete Sequence ◽  
Light Chains ◽  
Rabbit Antibody ◽  
Arginine Residues ◽  
V Region ◽  
Combination Of Methods

The amino acid sequence of the N-terminal 139 residues of the L (light) chain derived from a homogeneous rabbit antibody (designated BS-1) to type III pneumococci was determined. A combination of methods involving tryptic cleavage restricted to the 2 arginine residues of the molecule and mild acid hydrolysis of a labile peptide bond between the V (variable) and C (constant) regions of the L chain (Fraser et al., 1972) allowed the isolation of two large peptides comprising the entire V region (residues 1–109); these peptides were suitable for automated Edman degradation. The complete sequence analysis of the V region was carried out with only 4μmol of L chain. This material was homogeneous, although minor variant sequences, if present at the 10% value, would not have been detected. The L chain contains 3 intrachain disulphide bridges, whose pairing was established by diagonal electrophoresis: there is one V-region bridge between positions 23 and 88 and one C-region bridge between positions 134 and 194; the third one connects V and C domains between positions 80 and 171. When compared with the basic sequence of human κ chains, rabbit L chain BS-1 appears to be more similar to the VKI prototype sequence than to VKII or VKIII sequences, where VKI, VKII and VKIII represent subgroups I, II and III respectively of V regions of κ light chains. The V regions of rabbit heavy and light chains are homologous to each other. The presence of two clusters of 3 glycine residues in positions 94–96 and 99–101 respectively is remarkable. Residues 94–96 may be related to antibody complementarity whereas residues 99–101 function probably as a pivot permitting the combining region of the L chain to make optimal contact with the antigenic determinant (Wu & Kabat, 1970).

scholarly journals The V-region sequence of the H chain from a third rabbit anti-pneumococcal antibody

1976 ◽  
Vol 157 (2) ◽  
pp. 449-459 ◽  
Author(s):  
J C Jaton
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Sequence Data ◽  
Hypervariable Region ◽  
Variable Region ◽  
Amino Acid Sequences ◽  
Rabbit Antibody ◽  
Simple Correlation ◽  
Type Iii ◽  
V Region

The amino acid sequence of the V (variable) region of the heavy (H) chain of rabbit antibody BS-1, raised against type III pneumococcal vaccine, is reported. Together with the sequence data of the V region of the light (L) chain previously determined [Jaton (1974a) Biochem. J. 141, 1-13], the present work completes the analysis of the V domain of the homogeneous antibody BS-1. The V domains (VL + VH regions) of this antibody are compared with those of two other anti-(type III) pneumococcal antibodies BS-5 and K-25 [Jaton (1975) Biochem. J. 147, 235-247]. Except for the second hypervariable section of the L chains, these antibodies have very different sequences in the hypervariable segments of the V domains. Within the third hypervariable region of the H chain, each antibody has a different length: BS-1 is three amino acids shorter than K-25 and two amino acids shorter than BS-5. When the sequences in that section are aligned for maximal homology, only two residues, glycine-97 and leucine-101, are common to the three antibodies. On the basis of the amino acid sequences of these three anti-pneumococcal antibodies, the results do not support the concept of a simple correlation between primary structure in the hypervariable sections (known to determine the shape of the combining site) and antigen-binding specificity.

scholarly journals Comparison of the amino acid sequences of the variable domains of two homogeneous rabbit antibodies to type III pneumococcal polysaccharide

1975 ◽  
Vol 147 (2) ◽  
pp. 235-247 ◽  
Author(s):  
J C Jaton
Keyword(s):  
Amino Acid ◽  
Complete Sequence ◽  
Amino Acid Sequences ◽  
Light Chains ◽  
Amino Acid Residues ◽  
Rabbit Antibody ◽  
Variable Regions ◽  
Type Iii ◽  
Variable Domains ◽  
V Region

The amino acid sequences of the V (variable) regions of the H (heavy) and L (light) chains derived from rabbit antibody K-25, specific for type III pneumococci, were determined; this is the second homogeneous rabbit antibody besides antibody BS-5 whose complete sequence of the V domain has been established (Jaton, 1974d). The V regions of L chains BS-5 and K-25 (both of allotype b4) differ from each other by 19 amino acid residues; 11 of these 19 substitutions are located within the three hypervariable sections of the V region. On the basis of seven amino acid differences within the N-terminal 28 positions, it is suggested that L chain K-25 belongs to a different subgroup of rabbit K chains and L chain BS-5. H chain K-25 (allotype a2) differs from another H chain of the same allotype by one amino acid substitution within the N-terminal 70 positions in addition to interchanges occurring in the first two hypervariable sections. H chain K-25 was compared with H chain BS-5 (allotype a1) and with the known V-region rabbit sequences. Allotype-related differences between a1, a2 and a3 chains appear to occur within the N-terminal 16 positions and possibly in scattered positions throughout the V-region. In the hypervariable positions, variability between the two antibodies is remarkably more pronounced within the third hypervariable section of both H and L chains than within the first two.

scholarly journals Partial amino acid sequence in the N-terminal region of an anti-pneumococcal immunoglobulin heavy chain of allotype a2

1974 ◽  
Vol 139 (1) ◽  
pp. 281-283 ◽  
Author(s):  
Jean-Claude Jaton ◽  
Joseph Haimovich
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Heavy Chain ◽  
Immunoglobulin Heavy Chain ◽  
Amino Acid Sequences ◽  
Terminal Region ◽  
Sequence Variability ◽  
Rabbit Antibody ◽  
Partial Amino Acid Sequence ◽  
Heavy Chains

The amino acid sequence of the N-terminal 48 residues of the heavy chain derived from a homogeneous rabbit antibody to type III pneumococci is described. This chain of allotype a2 is compared with other rabbit heavy chains of allotypes a1, a2 and a3. Within the N-terminal 25 positions, two chains which carry the same allotype a2 possess identical amino acid sequences, but differ markedly from heavy chains of allotypes a1 and a3. Sequence variability is observed in residues 26–27 and 30–34, but not in residues 35–48.

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