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The Amino Acid Following an Asn-X-Ser/Thr Sequon Is an Important Determinant of N-Linked Core Glycosylation Efficiency

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Department of Pathology, Johns Hopkins University School of Medicine, Baltimore, Maryland, Department of Pathology, Case Western Reserve University School of Medicine, Cleveland, Ohio, and Department of Pathology and Laboratory Medicine, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania
Cite this: Biochemistry 1998, 37, 19, 6833–6837
Publication Date (Web):April 22, 1998
https://doi.org/10.1021/bi972217k
Copyright © 1998 American Chemical Society
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    Abstract

    Many eukaryotic proteins are modified by Asn-linked (N-linked) glycosylation. The number and position of oligosaccharides added to a protein by the enzyme oligosaccharyltransferase can influence its expression and function. N-Linked glycosylation usually occurs at Asn residues in Asn-X-Ser/Thr sequons where X ≠ Pro. However, many Asn-X-Ser/Thr sequons are not glycosylated or are glycosylated inefficiently. Inefficient glycosylation at one or more Asn-X-Ser/Thr sequons in a protein results in the production of heterogeneous glycoprotein products. These glycoforms may differ from one another in their level of expression, stability, antigenicity, or function. The signals which control the efficiency of N-linked glycosylation at individual Asn residues have not been fully defined. In this report, we use a site-directed mutagenesis approach to investigate the influence of the amino acid at the position following a sequon (the Y position, Asn-X-Ser/Thr-Y). Variants of rabies virus glycoprotein containing a single Asn-X-Ser/Thr sequon at Asn37 were generated. Variants were designed with each of the twenty common amino acids at the Y position, with either Ser or Thr at the hydroxy (Ser/Thr) position. The core glycosylation efficiency of each variant was quantified using a cell-free translation/glycosylation system. These studies reveal that the amino acid at the Y position is an important determinant of core glycosylation efficiency.

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    ‡

     Johns Hopkins University School of Medicine.

    §

     Case Western Reserve University School of Medicine.

    ‖

     University of Pennsylvania School of Medicine.

    *

     To whom correspondence should be addressed:  Department of Pathology, Ross Bldg. 646, Johns Hopkins Medical Institutions, 720 Rutland Ave., Baltimore, MD 21205. Phone:  (410) 614-4734. Fax:  (410) 614-3548. E-mail:  [email protected].

    †

     This work was supported in part by Grants CH/HD-34348-01A1 (S.E.) and T32-GM08056 (J.M.) from the National Institutes of Health.

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