Recognition of microbial glycans by human intelectin-1

Wesener, Darryl A.; Wangkanont, Kittikhun; McBride, Ryan; Song, Xuezheng; Kraft, Matthew B.; Hodges, Heather L.; Zarling, Lucas C.; Splain, Rebecca A.; Smith, David F.; Cummings, Richard D.; Paulson, James C.; Forest, Katrina T.; Kiessling, Laura L.

doi:10.1038/nsmb.3053

Title: Recognition of microbial glycans by human intelectin-1

Journal Article · Mon Jul 06 00:00:00 EDT 2015 · Nature Structural & Molecular Biology

DOI:https://doi.org/10.1038/nsmb.3053· OSTI ID:1214864

Wesener, Darryl A. ^[1];

^[2]; McBride, Ryan ^[3]; Song, Xuezheng ^[4]; Kraft, Matthew B. ^[2]; Hodges, Heather L. ^[2]; Zarling, Lucas C. ^[1]; Splain, Rebecca A. ^[2]; Smith, David F. ^[4]; Cummings, Richard D. ^[4]; Paulson, James C. ^[3]; Forest, Katrina T. ^[5]; Kiessling, Laura L. ^[6]

Univ. of Wisconsin, Madison, WI (United States). Dept. of Biochemistry
Univ. of Wisconsin, Madison, WI (United States). Dept. of Chemistry
Scripps Research Inst., La Jolla, CA (United States). Dept. of Cell and Molecular Biology. Dept. of Chemical Physiology
Emory Univ., Atlanta, GA (United States). School of Medicine. Dept. of Biochemistry. Glycomics Center
Univ. of Wisconsin, Madison, WI (United States). Dept. of Bacteriology
Univ. of Wisconsin, Madison, WI (United States). Dept. of Biochemistry. Dept. of Chemistry

The glycans displayed on mammalian cells can differ markedly from those on microbes. Such differences could, in principle, be 'read' by carbohydrate-binding proteins, or lectins. In this paper, we used glycan microarrays to show that human intelectin-1 (hIntL-1) does not bind known human glycan epitopes but does interact with multiple glycan epitopes found exclusively on microbes: β-linked D-galactofuranose (β-Galf), D-phosphoglycerol–modified glycans, heptoses, D-glycero-D-talo-oct-2-ulosonic acid (KO) and 3-deoxy-D-manno-oct-2-ulosonic acid (KDO). The 1.6-Å-resolution crystal structure of hIntL-1 complexed with β-Galf revealed that hIntL-1 uses a bound calcium ion to coordinate terminal exocyclic 1,2-diols. N-acetylneuraminic acid (Neu5Ac), a sialic acid widespread in human glycans, has an exocyclic 1,2-diol but does not bind hIntL-1, probably owing to unfavorable steric and electronic effects. hIntL-1 marks only Streptococcus pneumoniae serotypes that display surface glycans with terminal 1,2-diol groups. Finally, this ligand selectivity suggests that hIntL-1 functions in microbial surveillance.

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Research Organization:: Univ. of Wisconsin, Madison, WI (United States)

Sponsoring Organization:: USDOE; National Inst. of Health (NIH) (United States); National Science Foundation (NSF); Michigan Economic Development Corporation (United States); Michigan Technology Tri-Corridor (United States)

Contributing Organization:: Scripps Research Inst., La Jolla, CA (United States); Emory Univ., Atlanta, GA (United States)

Grant/Contract Number:: AC02-06CH11357; R01GM55984; R01AI063596; T32 GM008505; F32 GM100729; GM062116; GM98791; P41GM103694; BIR-9512577; S10 RR13790; P30 CA014520; 1S10RR024715; CHE-9208463; CHE-9629688; 1S10RR08389; 085P1000817

OSTI ID:: 1214864

Journal Information:: Nature Structural & Molecular Biology, Vol. 22, Issue 8; ISSN 1545-9993

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: ENGLISH

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Cited by: 109 works

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