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Open AccessJournal ArticleDOI

Content and organization of the human Ig VH locus: definition of three new VH families and linkage to the Ig CH locus.

TLDR
The first report of the physical linkage of the variable and constant loci of a human Ig gene family is provided by demonstrating that the most proximal known human VH segments lie within 100 kb of the constant region locus.
Abstract
We present a detailed analysis of the content and organization of the human immunoglobulin VH locus. Human VH genes representing five distinct families were isolated, including novel members belonging to two out of three of the known VH gene families (VH1 and VH3) as well as members of three new families (VH4, VH5, and VH6). We report the nucleotide sequence of 21 novel human VH genes, many of which belong to the three new VH gene families. In addition, we provide a preliminary analysis of the organization of these gene segments over the full extent of the locus. We find that the five multi-segment families (VH1-5) have members interspersed over nearly the full 1500-2000 kb of the VH locus, and estimate that the entire heavy chain locus covers 2500 kb or less. Finally, we provide the first report of the physical linkage of the variable and constant loci of a human Ig gene family by demonstrating that the most proximal known human VH segments lie within 100 kb of the constant region locus.

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A novel domain antibody rationally designed against TNF-α using variable region of human heavy chain antibody as scaffolds to display antagonistic peptides

TL;DR: It is shown that it is possible to screen potential antagonists of TNF-alpha using in vitro analysis systems in combination with the computer-aided modeling method and was significantly stronger than three peptides displayed by ATD5.
Journal ArticleDOI

Isolation and sequence of a cDNA codig for the immunoglobulin μ chain of the sheep

TL;DR: A sheep cDNA library was screened with a human C mu probe, and the complete nucleotide sequence of a 1923 nt cDNA was determined as discussed by the authors, which contains sequences corresponding to all the exons (VH, DH, JH, CH1, CH2, CH3 and CH4) characteristic of the immunoglobulin mu heavy chain regions.
Journal ArticleDOI

The Alternative Binding Site for Protein A in the Fab Fragment of Immunoglobulins

TL;DR: Twenty‐six new human or murine monoclonal immunoglobulins (IgM, IgA, murine IgGl or human IgG3) with a known V‐region sequence were tested for alternative (non‐Fc) binding to Staphylococcal protein A and fifteen immunoglOBulins were found to bind more firmly.
Journal ArticleDOI

DNA sequence analysis and comparison of the variable heavy and light chain regions of two IgM, monoclonal, anti-myelin associated glycoprotein antibodies.

TL;DR: Comparative analysis of the two VH regions has revealed that they are 88% homologous to one another and are both members of the VH3 gene family, and highly homologueous to a gene which is frequently utilized in the fetal B-cell repertoire.
Journal ArticleDOI

The early expression of some human autoantibody-associated heavy chain variable region genes is controlled by specific regulatory elements

TL;DR: It is hypothesized that these autoantibody‐related Vh genes may contain various combinations of cis regulatory elements which infiuence their specific expression during early ontogenic development, which is consistent with network hypotheses, which suggest that early B‐cell development is driven by reactivity with self.
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