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Cited by 1,340Monoclonal and Polyclonal Antibodies ResearchMultiple Myeloma Research and TreatmentsProtein Structure and Dynamics

An analysis of the sequences of the variable regions of Bence Jones proteins and myeloma light chains and their implications for antibody complementarity

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Wu, Tai Te, Kabat, Elvin A.·1970·The Journal of Experimental Medicine
DOI 10.1084/jem.132.2.211PMC PMC2138737
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Abstract

In an attempt to account for antibody specificity and complementarity in terms of structure, human kappa-, human lambda-, and mouse kappa-Bence Jones proteins and light chains are considered as a single population and the variable and constant regions are compared using the sequence data available. Statistical criteria are used in evaluating each position in the sequence as to whether it is essentially invariant or group-specific, subgroup-specific, species-specific, etc. Examination of the invariant residues of the variable and constant regions confirms the existence of a large number of invariant glycines, no invariant valine, lysine, and histidine, and only one invariant leucine and alanine in the variable region, as compared with the absence of invariant glycines and presence of three each of invariant alanine, leucine, and valine and two each of invariant lysine and histidine in the constant region. The unique role of glycine in the variable region is emphasized. Hydrophobicity of the invariant residues of the two regions is also evaluated. A parameter termed variability is defined and plotted against the position for the 107 residues of the variable region. Three stretches of unusually high variability are noted at residues 24-34, 50-56, and 89-97; variations in length have been found in the first and third of these. It is hypothesized that positions 24-34 and 89-97 contain the complementarity-determining residues of the light chain-those which make contact with the antigenic determinant. The heavy chain also has been reported to have a similar region of very high variability which would also participate in forming the antibody-combining site. It is postulated that the information for site complementarity is contained in some extrachromosomal DNA such as an episome and is incorporated by insertion into the DNA of the structural genes for the variable region of short linear sequences of nucleotides. The advantages and disadvantages of this hypothesis are discussed.

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  • Kabat and IMGT definitions are based on sequence alignments identifying conserved positions in the variable region whereas Chothia takes into account the 3D structure of the CDR loops.

    “Kabat and IMGT definitions are based on sequence alignments identifying conserved positions in the variable region [152, 153] whereas Chothia takes into account the 3D structure of the CDR loops.”

    From Computational approaches to therapeutic antibody design: established methods and emerging trends (2020) · cites this paper as [152]

  • Since the seminal work to define a standard numbering scheme for antibodies was carried out by Kabat in 1970, the Chothia and IMGT schemes have been adopted as the main alternatives.

    “Since the seminal work to define a standard numbering scheme for antibodies was carried out by Kabat in 1970 [152], the Chothia [32] and IMGT [153] schemes have been adopted as the main alternatives.”

    From Computational approaches to therapeutic antibody design: established methods and emerging trends (2020) · cites this paper as [152]

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Authors
Wu, T. T., & Kabat, E. A.
Affiliations
NewYork–Presbyterian Hospital (US)
Venue
The Journal of Experimental Medicine
Publisher
Rockefeller University Press
Published
1970-08-01
Volume
132
Issue
2
Pages
211-250
ISSN
  • 0022-1007 (ISSN-L)
  • 1540-9538
DOI
10.1084/jem.132.2.211
PMC
PMC2138737
OpenAlex
W2127552260
Cited by
1,340
References
72
Citations by year
2026: 18 · 2025: 17 · 2024: 33 · 2023: 22 · 2022: 24 · 2021: 28 · 2020: 28 · 2019: 30 · 2018: 21 · 2017: 25 · 2016: 31 · 2015: 32 · 2014: 34 · 2013: 35 · 2012: 28
FWCI
65.83
Type
journal article
Language
en
Open access
Locations
  • The Journal of Experimental Medicine (publishedVersion)
  • PubMed Central (publishedVersion, cc-by-nc-sa)
  • PubMed (publishedVersion)
Funders
  • National Science Foundation (GB-8341)
  • National Cancer Institute (CA08748)
Topics
  • Health Sciences › Medicine › Radiology, Nuclear Medicine and Imaging › Monoclonal and Polyclonal Antibodies Research
  • Health Sciences › Medicine › Hematology › Multiple Myeloma Research and Treatments
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords
Bence Jones protein, immunoglobulin variable region, hypervariable region, invariant residues, glycine, hydrophobicity, sequence variation, kappa light chain, lambda light chain, episomes, antibody combining site, antigenic determinants
MeSH terms
Alanine, Amino Acid Sequence, Analysis of Variance, Animals, Antibodies, Antibody Specificity, Bence Jones Protein, Binding Sites, Genes, Glycine, Histidine, Humans, Immunoglobulin G, Immunoglobulin M, Leucine, Lysine, Models, Chemical, Multiple Myeloma, Rabbits, Species Specificity, Valine, Mice

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