Evidence map›Paper›PMID 38713874›Full record

ArticleAngewandte Chemie (International ed. in English)2024

Synthetic Sialosides Terminated with 8-N-Substituted Sialic Acid as Selective Substrates for Sialidases from Bacteria and Influenza Viruses.

Bijoyananda Mishra, Yue Yuan, Hai Yu, Hyeog Kang, Jin Gao, Robert Daniels, Xi Chen

Abstract read
In one paragraph

Article in Angewandte Chemie (International ed. in English), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

3 citing papers in PubMed.

  1. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Bijoyananda MishraDepartment of Chemistry, University of California, One Shields Avenue, Davis, California, 95616, United States.ORCID 0000-0002-6777-9341
Yue YuanDepartment of Chemistry, University of California, One Shields Avenue, Davis, California, 95616, United States.ORCID 0000-0003-3524-0576
Hai YuDepartment of Chemistry, University of California, One Shields Avenue, Davis, California, 95616, United States.ORCID 0000-0002-4378-0532
Hyeog KangDivision of Viral Products, Center for Biologics Evaluation and Research, Food and Drug Administration, Silver Spring, Maryland, 20993, United States.ORCID 0000-0001-8935-1103
Jin GaoDivision of Viral Products, Center for Biologics Evaluation and Research, Food and Drug Administration, Silver Spring, Maryland, 20993, United States.ORCID 0000-0002-8019-9210
Robert DanielsDivision of Viral Products, Center for Biologics Evaluation and Research, Food and Drug Administration, Silver Spring, Maryland, 20993, United States.ORCID 0000-0002-5988-2920
Xi ChenDepartment of Chemistry, University of California, One Shields Avenue, Davis, California, 95616, United States.ORCID 0000-0002-3160-614X

Funding

Supplement: Exploring the biology of O-acetyl sialic acids using stable synthetic mimicsR01AI130684 · NIAID · UNIVERSITY OF CALIFORNIA AT DAVIS · PI CHEN, XI, VARKI, AJIT P · 2017 to 2020
$2.3M
Chemoenzymatic synthesis of bacterial nonulosonic acids and glycansR01GM141324 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI CHEN, XI · 2021 to 2024
$1.2M
Acquisition of a Q-Exactive Plus Mass SpectrometerS10OD025271 · OD · UNIVERSITY OF CALIFORNIA AT DAVIS · PI JEWELL, WILLIAM T · 2019 to 2019
$486k
National Institute of Allergy and Infectious Diseases R01AI130684NIAID NIH HHS R01 AI130684NIGMS NIH HHS R01 GM141324NIGMS NIH HHS R01GM141324NIH HHS S10 OD025271Office of Research Infrastructure Programs, National Institutes of Health S10OD025271
6 · The paper itself

Abstract

Sialosides containing C8-modified sialic acids are challenging synthetic targets but potentially useful probes for diagnostic substrate profiling of sialidases and elucidating the binding specificity of sialic acid-interacting proteins. Here, we demonstrate efficient chemoenzymatic methods for synthesizing para-nitrophenol-tagged α2-3- and α2-6-linked sialyl galactosides containing C8-acetamido, C8-azido, or C8-amino derivatized N-acetylneuraminic acid (Neu5Ac). High-throughput substrate specificity studies showed that the C8-modification of sialic acid significantly changes its recognition by sialidases from humans, various bacteria, and different influenza A and B viruses. Sialosides carrying Neu5Ac with a C8-azido modification were generally well tolerated by all the sialidases we tested, whereas sialosides containing C8-acetamido-modified Neu5Ac were only cleaved by selective bacterial sialidases. In contrast, sialosides with C8-amino-modified Neu5Ac were cleaved by a combination of selective bacterial and influenza A virus sialidases. These results indicate that sialosides terminated with a C8-amino or C8-acetamido-modified sialic acid can be used with other sialosides for diagnostic profiling of disease-causing sialidase-producing pathogens.

Indexed as

NeuraminidaseSialic AcidsBacteriaHumansInfluenza A virusN-Acetylneuraminic AcidOrthomyxoviridaeSubstrate SpecificityN-Acetylneuraminic AcidNeuraminidaseSialic Acids8-substituted sialic acidscarbohydrateschemoenzymatic synthesisinfluenza virussialidase

Identifiers

PMID38713874
PMCPMC11288309

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.