Characterization of horse (Equus caballus) immunoglobulin mu chain-encoding genes.
Abstract: Horse (Equus caballus) immunoglobulin mu chain-encoding (IgM) variable, joining, and constant gene segments were cloned and characterized. Nucleotide sequence analyses of 15 cDNA clones from a mesenteric lymph node library identified 7 unique variable gene segments, 5 separate joining segments, and a single constant region. Based on comparison with human sequences, horse variable segments could be grouped into either family 1 of immunoglobulin (Ig) clan I or family 4 of Ig clan II subclan IV. All horse sequences had a relatively conserved 16 base pair (bp) segment in framework 3 which was recognized with high specificity in polymerase chain reaction by a degenerate oligonucleotide primer. Horse complementarity determining regions (CDR) had considerable variability in predicted amino acid content and length but also included the presence of relatively conserved residues and several canonical sequences that may be necessary in formation of the beta chain main structure and conformation of antigen-binding sites through interaction with light chain CDR. Sequence analysis of joining regions revealed the presence of nearly invariant 3' regions similar to those found in human and mouse genes. A single horse IgM constant region comprising 1472 bp and encoding 451 residues was also identified. Direct comparison of the horse constant region predicted amino acid sequence with those from eleven other species revealed the presence of 53 invariant residues with particularly conserved sequences within the third and fourth exons. Phylogenetic analysis using a neighbor-joining algorithm showed closest similarity of the horse mu chain-encoding constant region gene to human and dog sequences. Together, these findings provide insights into the comparative biology of IgM as well as data for additional detailed studies of the horse immune system and investigation of immune-related diseases.
Publication Date: 1997-01-01 PubMed ID: 9089096DOI: 10.1007/s002510050220Google Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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The research focuses on decoding and examining the horse immunoglobulin mu chain-encoding (IgM) genes to better comprehend the IgM and horse immune system.
Study Design and Methodology
- The researchers acquired immunoglobulin mu chain-encoding (IgM) variable, joining, and constant gene segments from horses, then cloned and analyzed them.
- Through nucleotide sequence analyses of 15 cDNA clones from a mesenteric lymph node library, they identified 7 unique variable gene segments, 5 separate joining segments, and a singular constant region.
- The gene segments were then compared to human sequences to classify them into immunoglobulin (Ig) families.
Findings
- Through comparison with human sequences, the horse variable segments were grouped into either family 1 of immunoglobulin (Ig) clan I or family 4 of Ig clan II subclan IV.
- All horse sequences displayed a relatively preserved 16 base pair (bp) segment in framework 3, which was identified with high specificity in the polymerase chain reaction by a degenerate oligonucleotide primer.
- Horse complementarity determining regions (CDR), demonstrated considerable variation in predicted amino acid content and length.
- Among this variability, it was found that they also included the presence of comparatively conserved residues and several canonical sequences that may be crucial in the formation of the beta chain main structure and formation of antigen-binding sites through the interaction with the light chain CDR.
- Sequence analysis of joining regions showed nearly invariant 3′ regions analogous to those found in human and mouse genes.
- The researchers also identified a single horse IgM constant region consisting of 1472 base pairs and encoding 451 residues.
- A direct comparison of the horse constant region predicted amino acid sequence with those from eleven other species revealed the presence of 53 invariant residues with particularly conserved sequences within the third and fourth exons.
Comparative Analysis
- A phylogenetic examination using a neighbor-joining algorithm illustrated closest similarity of the horse mu chain-encoding constant region gene to human and dog sequences.
Conclusion
- The results offer insights into the comparative biology of IgM, and provide data for more comprehensive studies of the horse immune system.
- The findings hold potential for aiding the investigation of immune-related diseases.
Cite This Article
APA
Schrenzel MD, King DP, McKnight ML, Ferrick DA.
(1997).
Characterization of horse (Equus caballus) immunoglobulin mu chain-encoding genes.
Immunogenetics, 45(6), 386-393.
https://doi.org/10.1007/s002510050220 Publication
Researcher Affiliations
- Department of Pathology, Microbiology, Immunology, School of Veterinary Medicine, University of California, Davis, CA 95616, USA.
MeSH Terms
- Amino Acid Sequence
- Animals
- Base Sequence
- Cloning, Molecular
- Dogs
- Horses
- Humans
- Immunoglobulin mu-Chains / genetics
- Mice
- Molecular Sequence Data
- Sequence Alignment
Citations
This article has been cited 4 times.- Tallmadge RL, Tseng CT, King RA, Felippe MJ. Developmental progression of equine immunoglobulin heavy chain variable region diversity.. Dev Comp Immunol 2013 Sep;41(1):33-43.
- Guo Y, Bao Y, Wang H, Hu X, Zhao Z, Li N, Zhao Y. A preliminary analysis of the immunoglobulin genes in the African elephant (Loxodonta africana).. PLoS One 2011 Feb 25;6(2):e16889.
- Wagner B, Greiser-Wilke I, Antczak DF. Characterization of the horse (Equus caballus) IGHA gene.. Immunogenetics 2003 Nov;55(8):552-60.
- Zhao Y, Hammarström L. Cloning of the complete rat immunoglobulin delta gene: evolutionary implications.. Immunology 2003 Mar;108(3):288-95.
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