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Microbial binding module employs sophisticated clustered saccharide patches to selectively adhere to mucins

Here, authors provide a molecular view of a clustered saccharide patch on mucins as recognized by a bacterial binding module. This work provides insights into how microbes can remain attached to mucins in the mucus while grazing on their glycans.

Thapakorn Jaroentomeechai
Billy Veloz
Yoshiki Narimatsu
ResearchOpen Access13 Oct 2025
Nature Communications

Volume: 16, P: 1-14
Structure-guided phage display discovery of antibodies for (S)Tn-glycans in protein context

Structural studies of certain Tn and STn antigen-targeting antibodies reveal that their V_H and V_L domains recognize the glycan antigen and the adjacent peptide region, respectively, enabling a V_H domain-focused and V_L domain-varying phage display library to generate antibodies targeting diverse glycopeptide epitopes.

Ramon Hurtado-Guerrero
Spyridon Gatos
Ola Blixt
Research31 Jul 2025
Nature Chemical Biology

P: 1-12
Structural basis for the synthesis of the core 1 structure by C1GalT1

The glycosyltransferase C1GalT1 directs a key step in protein O-glycosylation important for the expression of the cancer-associated Tn and T antigens. Here, the authors provide molecular insights into the function of C1GalT1 by solving the crystal structure of the Drosophila enzyme-substrate complex.

Andrés Manuel González-Ramírez
Ana Sofia Grosso
Ramon Hurtado-Guerrero
ResearchOpen Access03 May 2022
Nature Communications

Volume: 13, P: 1-15
Structural and mechanistic insights into the cleavage of clustered O-glycan patches-containing glycoproteins by mucinases of the human gut

AM0627 is a bis-O-glycan mucinase that might work in the final steps of mucus degradation, thereby providing a carbon and nitrogen source for Akkermansia muciniphila. Here, the authors provide molecular insights into AM0627 function from X-ray crystallography and computer simulations.

Víctor Taleb
Qinghua Liao
Ramon Hurtado-Guerrero
ResearchOpen Access26 Jul 2022
Nature Communications

Volume: 13, P: 1-15
Molecular basis for fibroblast growth factor 23 O-glycosylation by GalNAc-T3

Polypeptide GalNAc-transferase T3 catalyzes the specific glycosylation of threonine-178 of fibroblast growth factor 23, and structural insights reveal a unique lectin-based mechanism of substrate recognition.

Matilde de las Rivas
Earnest James Paul Daniel
Ramon Hurtado-Guerrero
Research13 Jan 2020
Nature Chemical Biology

Volume: 16, P: 351-360
Author Correction: Molecular basis for bacterial N-glycosylation by a soluble HMW1C-like N-glycosyltransferase

Beatriz Piniello
Javier Macías-León
Ramon Hurtado-Guerrero
Amendments and CorrectionsOpen Access13 Feb 2024
Nature Communications

Volume: 15, P: 1
A family of di-glutamate mucin-degrading enzymes that bridges glycan hydrolases and peptidases

Mucins are glycosylated proteins with important biological functions such as protection. Although glycopeptidases can cleave them, dedicated hydrolytic enzymes specific for mucins were unknown. Now microbial mucinases are discovered that specifically recognize mucin O-glycan clusters and employ two glutamic acid residues for catalytic cleavage.

Yoshiki Narimatsu
Christian Büll
Ramon Hurtado-Guerrero
Research23 Feb 2024
Nature Catalysis

Volume: 7, P: 386-400
Molecular basis for bacterial N-glycosylation by a soluble HMW1C-like N-glycosyltransferase

NGTs glycosylate asparagine residues in proteins, crucial for bacterial adhesion and pathogenicity. Here, the authors provide insights via crystallography and simulations, showing acceptor asparagine uses imidic form for catalysis and UDP-glucose phosphate group acts as general base.

Beatriz Piniello
Javier Macías-León
Ramon Hurtado-Guerrero
ResearchOpen Access18 Sept 2023
Nature Communications

Volume: 14, P: 1-15
Dynamic interplay between catalytic and lectin domains of GalNAc-transferases modulates protein O-glycosylation

Polypeptide GalNAc-transferases decorate proteins with dense arrays of O-glycans, which in the case of mucins are essential for their barrier functions. Here the authors present comprehensive structural studies that shed light on the molecular attributes that allow GalNAc-T2 to efficiently carry out dense O-glycosylation.

Erandi Lira-Navarrete
Matilde de las Rivas
Ramon Hurtado-Guerrero
ResearchOpen Access05 May 2015
Nature Communications

Volume: 6, P: 1-12
The interdomain flexible linker of the polypeptide GalNAc transferases dictates their long-range glycosylation preferences

GalNAc transferases’ (GalNAc-Ts) catalytic domains are connected to a lectin domain through a flexible linker. Here the authors present a structural analysis of GalNAc-T4 that implicates the linker region as modulator of the orientations of the lectin domain, which in turn imparts substrate specificity.

Matilde de las Rivas
Erandi Lira-Navarrete
Ramon Hurtado-Guerrero
ResearchOpen Access05 Dec 2017
Nature Communications

Volume: 8, P: 1-11
Efficient and irreversible antibody–cysteine bioconjugation using carbonylacrylic reagents

Site-selective modification of antibodies is useful for therapeutic and imaging applications. This protocol is an alternative to maleimide labeling in which cysteine reacts selectively and irreversibly with functionalized carbonylacrylic reagents.

Barbara Bernardim
Maria J. Matos
Gonçalo J. L. Bernardes
Protocols23 Nov 2018
Nature Protocols

Volume: 14, P: 86-99

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