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United States Department of Agriculture

Agricultural Research Service

Title: Cloning and Sequencing of Bovine Intercellular Adhesion Molecule (Icam)-3

Authors
item Lee, Eunkyung - IA STATE UNIV., AMES, IA
item Kehrli Jr, Marcus
item Dietz, Allan - FORMER USDA, ARS, NADC
item Bosworth, Brad
item Reinhardt, Timothy

Submitted to: Gene
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: January 20, 1996
Publication Date: N/A

Interpretive Summary: Cattle experience diseases (both infectious and non-infectious) of many causes during their lifetime. The research reported here identifies the DNA sequence for a gene that participates in the controlled movement of white blood cells into diseased tissues of cattle. The work reported here provides the foundation for the next step in producing a new generation of compounds, which may be used to regulate immune responses in veterinary medicine. The main benefit of this work will be future work where we will attempt to produce a recombinant form of the protein made by this gene that can be used to control disease in cattle. A potential benefit of this type of research would be less use of antibiotics in cattle to treat infectious diseases.

Technical Abstract: Bovine intercellular adhesion molecule (ICAM)-3, a ligand of the leukocyte integrin LFA-1 (CD11a/CD18) was sequenced and compared with human ICAMs. The 1635-bp bovine sequence codes for a protein of 544 amino acids. Bovine ICAM-3 has five immunoglobulin-like domains similar to human ICAM-1 and ICAM-3, and belongs to the immunoglobulin gene superfamily. The overall homology of the deduced amino acid sequence with human ICAM-3 and ICAM-1 is 61% and 58%, respectively. The predicted number and positions of cysteine residues are all conserved between bovine and human ICAM-3 amino acid sequences. Fifteen potential N-glycosylation sites in bovine ICAM-3 indicate that the protein is heavily glycosylates like human ICAM-3.

Last Modified: 10/25/2014
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