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Cloning of an integrin beta subunit exhibiting high homology with integrin beta 3 subunit.

ABSTRACT: cDNAs for another beta subunit of the integrin family were isolated with the aid of polymerase chain reaction and sequenced. The combined cDNA sequence is 3110 base pairs (bp) in size and has one long open reading frame of 2388 bp. The deduced amino acid sequence is similar to those of other integrin beta subunits but does not correspond to beta 1, beta 2, beta 3, or beta 4 subunits. This beta subunit is divided by a membrane-spanning domain into a large extracellular domain at the N-terminal side and a small intracellular domain at the C-terminal side. The extracellular domain has a cysteine-rich region that contains four repeats of 8-cysteine motifs. All 56 cysteine residues found in the extracellular domains of other mature beta subunits are present in this beta subunit. The beta subunit reported here has particularly high homology with the beta 3 subunit. The mRNA for the molecule is approximately 3.5 kbp in size and is expressed in various cell types. Other researchers have recently reported additional beta subunits that associate with the vitronectin receptor alpha subunit. The deduced amino acid sequence of this molecule contains the N-terminal partial amino acid sequence of one of these beta subunits, beta x. The beta subunit described herein seems to be identical to the beta x subunit and to function as the beta subunit of a vitronectin receptor.

SUBMITTER: Suzuki S

PROVIDER: S-EPMC54322 | biostudies-other | 1990 Jul

REPOSITORIES: biostudies-other

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Cloning of an integrin beta subunit exhibiting high homology with integrin beta 3 subunit.

Suzuki S S Huang Z S ZS Tanihara H H

Proceedings of the National Academy of Sciences of the United States of America 19900701 14

cDNAs for another beta subunit of the integrin family were isolated with the aid of polymerase chain reaction and sequenced. The combined cDNA sequence is 3110 base pairs (bp) in size and has one long open reading frame of 2388 bp. The deduced amino acid sequence is similar to those of other integrin beta subunits but does not correspond to beta 1, beta 2, beta 3, or beta 4 subunits. This beta subunit is divided by a membrane-spanning domain into a large extracellular domain at the N-terminal si ...[more]

PMID: 2371275

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Project description:We have previously reported that Foot-and-mouth disease virus (FMDV), which is virulent for cattle and swine, can utilize the integrin alpha(v)beta(3) as a receptor on cultured cells. Since those studies were performed with the human integrin, we have molecularly cloned the bovine homolog of the integrin alpha(v)beta(3) and have compared the two receptors for utilization by FMDV. Both the alpha(v) and beta(3) subunits of the bovine integrin have high degrees of amino acid sequence similarity to their corresponding human subunits in the ectodomains (96%) and essentially identical transmembrane and cytoplasmic domains. Within the putative ligand-binding domains, the bovine and human alpha(v) subunits have a 98.8% amino acid sequence similarity while there is only a 93% similarity between the beta(3) subunits of these two species. COS cell cultures, which are not susceptible to FMDV infection, become susceptible if cotransfected with alpha(v) and beta(3) subunit cDNAs from a bovine or human source. Cultures cotransfected with the bovine alpha(v)beta(3) subunit cDNAs and infected with FMDV synthesize greater amounts of viral proteins than do infected cultures cotransfected with the human integrin subunits. Cells cotransfected with a bovine alpha(v) subunit and a human beta(3) subunit synthesize viral proteins at levels equivalent to those in cells expressing both human subunits. However, cells cotransfected with the human alpha(v) and the bovine beta(3) subunits synthesize amounts of viral proteins equivalent to those in cells expressing both bovine subunits, indicating that the bovine beta(3) subunit is responsible for the increased effectiveness of this receptor. By engineering chimeric bovine-human beta(3) subunits, we have shown that this increase in receptor efficiency is due to sequences encoding the C-terminal one-third of the subunit ectodomain, which contains a highly structured cysteine-rich repeat region. We postulate that amino acid sequence differences within this region may be responsible for structural differences between the human and bovine beta(3) subunit, leading to more efficient utilization of the bovine receptor by this bovine pathogen.

Dataset Information

Cloning of an integrin beta subunit exhibiting high homology with integrin beta 3 subunit.

Publications

Cloning of an integrin beta subunit exhibiting high homology with integrin beta 3 subunit.

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