Functionally important glycosyltransferase gain and loss during catarrhine primate emergence.

Functionally important glycosyltransferase gain and loss during catarrhine primate emergence. Research Abstract Details 

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Functionally important glycosyltransferase gain and loss during catarrhine primate emergence. Abstract Text:

Chihiro Koike,Monica Uddin,Derek E Wildman,Edward A Gray,Massimo Trucco,Thomas E Starzl,Morris Goodman,

A glycosyltransferase, alpha1,3galactosyltransferase, catalyzes the terminal step in biosynthesis of Galalpha1,3Galbeta1-4GlcNAc-R (alphaGal), an oligosaccharide cell surface epitope. This epitope or antigenically similar epitopes are widely distributed among the different forms of life. Although abundant in most mammals, alphaGal is not normally found in catarrhine primates (Old World monkeys and apes, including humans), all of which produce anti-alphaGal antibodies from infancy onward. Natural selection favoring enhanced resistance to alphaGal-positive pathogens has been the primary reason offered to account for the loss of alphaGal in catarrhines. Here, we question the primacy of this immune defense hypothesis with results that elucidate the evolutionary history of GGTA1 gene and pseudogene loci. One such locus, GGTA1P, a processed (intronless) pseudogene (PPG), is present in platyrrhines, i.e., New World monkeys, and catarrhines but not in prosimians. PPG arose in an early ancestor of anthropoids (catarrhines and platyrrhines), and GGTA1 itself became an unprocessed pseudogene in the late catarrhine stem lineage. Strong purifying selection, denoted by low nonsynonymous substitutions per nonsynonymous site/synonymous substitutions per synonymous site values, preserved GGTA1 in noncatarrhine mammals, indicating that the functional gene product is subjected to considerable physiological constraint. Thus, we propose that a pattern of alternative and/or more beneficial glycosyltransferase activity had to first evolve in the stem catarrhines before GGTA1 inactivation could occur. Enhanced defense against alphaGal-positive pathogens could then have accelerated the replacement of alphaGal-positive catarrhines by alphaGal-negative catarrhines. However, we emphasize that positively selected regulatory changes in sugar chain metabolism might well have contributed in a major way to catarrhine origins.

Functionally important glycosyltransferase gain and loss during catarrhine primate emergence. Publishing Authors By Initials

C Koike,M Uddin,DE Wildman,EA Gray,M Trucco,TE Starzl,M Goodman,

For similar natural sciences: time: time factors research abstracts see: natural sciences: time: time factors research

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Functionally important glycosyltransferase gain and loss during catarrhine primate emergence. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Proceedings of the National Academy of Sciences of

VOLUME: 104

Page Numbers: 559-64

Journal Abbreviation: Proc. Natl. Acad. Sci. U.S.A.

ISSN: 0027-8424

DAY: 28

MONTH: 12

YEAR: 2006

Functionally important glycosyltransferase gain and loss during catarrhine primate emergence. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 7505876

Functionally important glycosyltransferase gain and loss during catarrhine primate emergence. Keywords Mesh Terms:

KEYWORDS: Time Factors

MESH TERMS: metabolism

Chemical & Substance for Abstract: Functionally important glycosyltransferase gain and loss during catarrhine primate emergence. Information

Substance Name: beta-D-galactosyl-N-acetylglucosaminylgl

Registry Number: EC 2.4.1.87

Grant and Affiliation Information for Functionally important glycosyltransferase gain and loss during catarrhine primate emergence.

AFFILIATION: Department of Surgery and Thomas E. Starzl Transplantation Institute, University of Pittsburgh School of Medicine, Pittsburgh, PA 15213, USA.

Country: United States

AGENCY: United States NIDDK

GRANT: R01DK64207

ACRONYM: DK

MEDLINETA: Proc Natl Acad Sci U S A

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ACCESSION NUMBER: DQ985360

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