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Article: Microbiota-induced regulatory T cells associate with

Godefroy, Emmanuelle / Barbé, Laure / Le Moullac-Vaidye, Béatrice / Rocher, Jézabel / Breiman, Adrien / Leuillet, Sébastien / Mariat, Denis / Chatel, Jean-Marc / Ruvoën-Clouet, Nathalie / Carton, Thomas / Jotereau, Francine / Le Pendu, Jacques

Frontiers in microbiology

2023 Volume 14, Page(s) 1123803

Abstract: The FUT2 α1,2fucosyltransferase contributes to the synthesis of fucosylated glycans used as attachment factors by several pathogens, including noroviruses and rotaviruses, that can induce life-threatening gastroenteritis in young children. ...

Abstract	The FUT2 α1,2fucosyltransferase contributes to the synthesis of fucosylated glycans used as attachment factors by several pathogens, including noroviruses and rotaviruses, that can induce life-threatening gastroenteritis in young children.
Language	English
Publishing date	2023-02-27
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2587354-4
ISSN	1664-302X
ISSN	1664-302X
DOI	10.3389/fmicb.2023.1123803
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Article: Extent of the protection afforded by histo-blood group polymorphism against rotavirus gastroenteritis in metropolitan France and French Guiana.

Masson, Lydie / Barbé, Laure / Henaff, Fanny / Ahmed, Tasnuva / Le Moullac-Vaidye, Béatrice / Peltier, Cécile / Marchand, Sarah S / Scherdel, Pauline / Vibet, Marie-Anne / Ruvoën-Clouet, Nathalie / Elenga, Narcisse / Imbert-Marcille, Berthe-Marie / Gras-Le Guen, Christèle / Le Pendu, Jacques

Frontiers in microbiology

2023 Volume 14, Page(s) 1141652

Abstract: Human rotaviruses attach to histo-blood group antigens glycans and null alleles of ... ...

Abstract	Human rotaviruses attach to histo-blood group antigens glycans and null alleles of the
Language	English
Publishing date	2023-03-10
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2587354-4
ISSN	1664-302X
ISSN	1664-302X
DOI	10.3389/fmicb.2023.1141652
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Article: FUT2, Secretor Status and FUT3 Polymorphisms of Children with Acute Diarrhea Infected with Rotavirus and Norovirus in Brazil

Loureiro Tonini, Marco André / Pires Gonçalves Barreira, Débora Maria / Bueno de Freitas Santolin, Luciana / Bondi Volpini, Lays Paula / Gagliardi Leite, José Paulo / Le Moullac-Vaidye, Béatrice / Le Pendu, Jacques / Cruz Spano, Liliana

Viruses. 2020 Sept. 25, v. 12, no. 10

2020

Abstract: Host susceptibility according to human histo-blood group antigens (HBGAs) is widely known for norovirus infection, but is less described for rotavirus. Due to the variable HBGA polymorphism among populations, we aimed to evaluate the association between ... ...

Abstract	Host susceptibility according to human histo-blood group antigens (HBGAs) is widely known for norovirus infection, but is less described for rotavirus. Due to the variable HBGA polymorphism among populations, we aimed to evaluate the association between HBGA phenotypes (ABH, Lewis and secretor status) and susceptibility to rotavirus and norovirus symptomatic infection, and the polymorphisms of FUT2 and FUT3, of children from southeastern Brazil. Paired fecal-buccal specimens from 272 children with acute diarrhea were used to determine rotavirus/norovirus genotypes and HBGAs phenotypes/genotypes, respectively. Altogether, 100 (36.8%) children were infected with rotavirus and norovirus. The rotavirus P[8] genotype predominates (85.7%). Most of the noroviruses (93.8%) belonged to genogroup II (GII). GII.4 Sydney represented 76% (35/46) amongst five other genotypes. Rotavirus and noroviruses infected predominantly children with secretor status (97% and 98.5%, respectively). However, fewer rotavirus-infected children were Lewis-negative (8.6%) than the norovirus-infected ones (18.5%). FUT3 single nucleotide polymorphisms (SNP) occurred mostly at the T59G > G508A > T202C > C314T positions. Our results reinforce the current knowledge that secretors are more susceptible to infection by both rotavirus and norovirus than non-secretors. The high rate for Lewis negative (17.1%) and the combination of SNPs, beyond the secretor status, may reflect the highly mixed population in Brazil.
Keywords	Norovirus ; Rotavirus ; antigens ; children ; diarrhea ; disease susceptibility ; genotype ; humans ; phenotype ; single nucleotide polymorphism ; Brazil
Language	English
Dates of publication	2020-0925
Publishing place	Multidisciplinary Digital Publishing Institute
Document type	Article
ZDB-ID	2516098-9
ISSN	1999-4915
ISSN	1999-4915
DOI	10.3390/v12101084
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Article ; Online: FUT2,

Viruses

2020 Volume 12, Issue 10

Abstract	Host susceptibility according to human histo-blood group antigens (HBGAs) is widely known for norovirus infection, but is less described for rotavirus. Due to the variable HBGA polymorphism among populations, we aimed to evaluate the association between HBGA phenotypes (ABH, Lewis and secretor status) and susceptibility to rotavirus and norovirus symptomatic infection, and the polymorphisms of
MeSH term(s)	Blood Group Antigens/genetics ; Brazil/epidemiology ; Caliciviridae Infections/epidemiology ; Caliciviridae Infections/genetics ; Caliciviridae Infections/virology ; Child ; Child, Preschool ; Diarrhea/epidemiology ; Diarrhea/genetics ; Diarrhea/virology ; Fucosyltransferases/genetics ; Genetic Predisposition to Disease/genetics ; Genotype ; Humans ; Infant ; Norovirus/genetics ; Norovirus/isolation & purification ; Phenotype ; Polymorphism, Single Nucleotide ; Rotavirus/genetics ; Rotavirus/isolation & purification ; Rotavirus Infections/epidemiology ; Rotavirus Infections/genetics ; Rotavirus Infections/virology ; Galactoside 2-alpha-L-fucosyltransferase
Chemical Substances	Blood Group Antigens ; Fucosyltransferases (EC 2.4.1.-) ; 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase (EC 2.4.1.65)
Language	English
Publishing date	2020-09-25
Publishing country	Switzerland
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2516098-9
ISSN	1999-4915 ; 1999-4915
ISSN (online)	1999-4915
ISSN	1999-4915
DOI	10.3390/v12101084
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Article ; Online: Host-Range Shift Between Emerging P[8]-4 Rotavirus and Common P[8] and P[4] Strains.

Khachou, Amira / Le Moullac-Vaidye, Béatrice / Peltier, Cécile / Breiman, Adrien / Imbert-Marcille, Berthe-Marie / Ruvoen-Clouet, Nathalie / Aouni, Mahjoub / Mastouri, Maha / Chouchane, Slaheddine / Le Pendu, Jacques

The Journal of infectious diseases

2020 Volume 222, Issue 5, Page(s) 836–839

Abstract: In Tunisia, we observed that rotavirus P[8]-3 and P[4] strains in young children with gastroenteritis associate with secretor histo-blood group phenotype. In contrast, the emerging P[8]-4 strain, representing 10% of cases, was exclusively found in ... ...

Abstract	In Tunisia, we observed that rotavirus P[8]-3 and P[4] strains in young children with gastroenteritis associate with secretor histo-blood group phenotype. In contrast, the emerging P[8]-4 strain, representing 10% of cases, was exclusively found in nonsecretor patients. Unlike VP8* from P[8]-3 and P[4] strains, the P[8]-4 VP8* protein attached to glycans from saliva samples regardless of the donor's secretor status. Interestingly, a high frequency of FUT2 enzyme deficiency (nonsecretor phenotype) was observed in the population. This may allow cocirculation of P[8]-3 and P[8]-4 strains in secretor and nonsecretor children, respectively.
MeSH term(s)	Child, Preschool ; Fucosyltransferases/genetics ; Genotype ; Host Specificity ; Humans ; Infant ; Infant, Newborn ; Phenotype ; Polysaccharides/metabolism ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/metabolism ; Rotavirus/genetics ; Rotavirus/physiology ; Rotavirus Infections/genetics ; Saliva ; Viral Nonstructural Proteins/genetics ; Viral Nonstructural Proteins/metabolism ; Virus Attachment ; Galactoside 2-alpha-L-fucosyltransferase
Chemical Substances	Polysaccharides ; RNA-Binding Proteins ; Viral Nonstructural Proteins ; NS35 protein, rotavirus (138414-65-0) ; Fucosyltransferases (EC 2.4.1.-)
Language	English
Publishing date	2020-03-19
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	3019-3
ISSN	1537-6613 ; 0022-1899
ISSN (online)	1537-6613
ISSN	0022-1899
DOI	10.1093/infdis/jiaa122
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Article ; Online: Histo-blood group antigen-binding specificities of human rotaviruses are associated with gastroenteritis but not with in vitro infection.

Barbé, Laure / Le Moullac-Vaidye, Béatrice / Echasserieau, Klara / Bernardeau, Karine / Carton, Thomas / Bovin, Nicolai / Nordgren, Johan / Svensson, Lennart / Ruvoën-Clouet, Nathalie / Le Pendu, Jacques

Scientific reports

2018 Volume 8, Issue 1, Page(s) 12961

Abstract: Human strains of rotavirus A (RVAs) recognize fucosylated glycans belonging to histo-blood group antigens (HBGAs) through their spike protein VP8*. Lack of these ligands due to genetic polymorphisms is associated with resistance to gastroenteritis caused ...

Abstract	Human strains of rotavirus A (RVAs) recognize fucosylated glycans belonging to histo-blood group antigens (HBGAs) through their spike protein VP8. Lack of these ligands due to genetic polymorphisms is associated with resistance to gastroenteritis caused by P[8] genotype RVAs. With the aim to delineate the contribution of HBGAs in the process, we analyzed the glycan specificity of VP8 proteins from various P genotypes. Binding to saliva of VP8* from P[8] and P[4] genotypes required expression of both FUT2 and FUT3 enzymes, whilst binding of VP8* from the P[14] genotype required FUT2 and A enzymes. We further defined a glycan motif, GlcNAcβ3Galβ4GlcNAc, recognized by P[6] clinical strains. Conversion into Lewis antigens by the FUT3 enzyme impaired recognition, explaining their lower binding to saliva of Lewis positive phenotype. In addition, the presence of neutralizing antibodies was associated with the presence of the FUT2 wild type allele in sera from young healthy adults. Nonetheless, in vitro infection of transformed cell lines was independent of HBGAs expression, indicating that HBGAs are not human RV receptors. The match between results from saliva-based binding assays and the epidemiological data indicates that the polymorphism of human HBGAs controls susceptibility to RVAs, although the exact mechanism remains unclear.
MeSH term(s)	Adolescent ; Adult ; Animals ; Blood Group Antigens/genetics ; Blood Group Antigens/metabolism ; Caco-2 Cells ; Chlorocebus aethiops ; Female ; Fucosyltransferases/genetics ; Fucosyltransferases/metabolism ; Gastroenteritis/genetics ; Gastroenteritis/metabolism ; Gastroenteritis/virology ; Humans ; Male ; Protein Binding ; RNA-Binding Proteins/genetics ; RNA-Binding Proteins/metabolism ; Rotavirus/genetics ; Rotavirus/metabolism ; Rotavirus Infections/genetics ; Rotavirus Infections/metabolism ; Vero Cells ; Viral Nonstructural Proteins/genetics ; Viral Nonstructural Proteins/metabolism ; Galactoside 2-alpha-L-fucosyltransferase
Chemical Substances	Blood Group Antigens ; RNA-Binding Proteins ; Viral Nonstructural Proteins ; NS35 protein, rotavirus (138414-65-0) ; Fucosyltransferases (EC 2.4.1.-) ; 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase (EC 2.4.1.65)
Language	English
Publishing date	2018-08-28
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-018-31005-4
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Article ; Online: Shared human/rabbit ligands for rabbit hemorrhagic disease virus.

Nyström, Kristina / Le Moullac-Vaidye, Béatrice / Ruvoën-Clouet, Nathalie / Le Pendu, Jacques

Emerging infectious diseases

2012 Volume 18, Issue 3, Page(s) 518–519

MeSH term(s)	Animals ; Blood Group Antigens/metabolism ; Caliciviridae Infections/metabolism ; Caliciviridae Infections/virology ; Epithelial Cells/metabolism ; Hemorrhagic Disease Virus, Rabbit/physiology ; Humans ; Ligands ; Rabbits ; Saliva/metabolism ; Viral Tropism ; Virus Attachment
Chemical Substances	Blood Group Antigens ; Ligands
Language	English
Publishing date	2012-02-27
Publishing country	United States
Document type	Letter ; Research Support, Non-U.S. Gov't
ZDB-ID	1380686-5
ISSN	1080-6059 ; 1080-6040
ISSN (online)	1080-6059
ISSN	1080-6040
DOI	10.3201/eid1803.111402
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Article: Association between expression of the H histo-blood group antigen, α1,2fucosyltransferases polymorphism of wild rabbits, and sensitivity to rabbit hemorrhagic disease virus

Guillon, Patrice / Ruvoën-Clouet, Nathalie / Le Moullac-Vaidye, Béatrice / Marchandeau, Stéphane / Le Pendu, Jacques

Glycobiology. 2009 Jan., v. 19, no. 1

2009

Abstract: RHDV (rabbit hemorrhagic disease virus) is a highly virulent calicivirus that has become a major cause of mortality in wild rabbit populations (Oryctolagus cuniculus). It binds to the histo-blood group antigen (HBGA) H type 2 which requires an α1, ... ...

Abstract	RHDV (rabbit hemorrhagic disease virus) is a highly virulent calicivirus that has become a major cause of mortality in wild rabbit populations (Oryctolagus cuniculus). It binds to the histo-blood group antigen (HBGA) H type 2 which requires an α1,2fucosyltransferase for its synthesis. In rabbit, three α1,2fucosyltransferases genes are known, Fut1, Fut2, and Sec1. Nonfunctional alleles at any of these loci could potentially confer resistance to RHDV, similar to human FUT2 alleles that determine the nonsecretor phenotype and resistance to infection by various NoV strains. In this study, we looked for the presence of H type 2 on buccal epithelial cells of wild rabbits from two geographic areas under RHDV pressure and from one RHDV-free area. Some animals with diminished H type 2 expression were found in the three populations (nonsecretor-like phenotype). Their frequency markedly increased according to the RHDV impact, suggesting that outbreaks selected survivors with low expression of the virus ligand. Polymorphisms of the Fut1, Fut2, and Sec1 coding regions were determined among animals that either died or survived outbreaks. The Fut2 and Sec1 genes presented a high polymorphism and the frequency of one Sec1 allele was significantly elevated, over 6-fold, among survivors. Sec1 enzyme variants showed either moderate, low, or undetectable catalytic activity, whereas all variant Fut2 enzymes showed strong catalytic activity. This functional analysis of the enzymes encoded by each Fut2 and Sec1 allele suggests that the association between one Sec1 allele and survival might be explained by a deficit of α1,2fucosyltransferase expression rather than by impaired catalytic activity.
Keywords	Oryctolagus cuniculus ; Rabbit hemorrhagic disease virus ; Vesivirus ; alleles ; antigens ; catalytic activity ; epithelial cells ; glycosyltransferases ; humans ; ligands ; loci ; mortality ; phenotype ; rabbits ; virulence ; viruses
Language	English
Dates of publication	2009-01
Size	p. 21-28.
Document type	Article
ZDB-ID	1067689-2
ISSN	1460-2423 ; 0959-6658
ISSN (online)	1460-2423
ISSN	0959-6658
DOI	10.1093/glycob/cwn098
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Article ; Online: Host-Specific Glycans Are Correlated with Susceptibility to Infection by Lagoviruses, but Not with Their Virulence.

Lopes, Ana M / Breiman, Adrien / Lora, Mónica / Le Moullac-Vaidye, Béatrice / Galanina, Oxana / Nyström, Kristina / Marchandeau, Stephane / Le Gall-Reculé, Ghislaine / Strive, Tanja / Neimanis, Aleksija / Bovin, Nicolai V / Ruvoën-Clouet, Nathalie / Esteves, Pedro J / Abrantes, Joana / Le Pendu, Jacques

Journal of virology

2018 Volume 92, Issue 4

Abstract: Rabbit hemorrhagic disease virus (RHDV) and European brown hare syndrome virus (EBHSV) are two lagoviruses from the ... ...

Abstract	Rabbit hemorrhagic disease virus (RHDV) and European brown hare syndrome virus (EBHSV) are two lagoviruses from the family
MeSH term(s)	Animals ; Caliciviridae Infections/metabolism ; Caliciviridae Infections/virology ; Disease Susceptibility ; Hares ; Hemorrhagic Disease Virus, Rabbit/physiology ; Lagomorpha/classification ; Lagomorpha/metabolism ; Lagomorpha/virology ; Lagovirus/physiology ; Phylogeny ; Polysaccharides/metabolism ; Rabbits ; Species Specificity ; Virulence ; Virus Attachment
Chemical Substances	Polysaccharides
Language	English
Publishing date	2018-01-30
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/JVI.01759-17
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Article ; Online: Neofunctionalization of the Sec1 α1,2fucosyltransferase paralogue in leporids contributes to glycan polymorphism and resistance to rabbit hemorrhagic disease virus.

Nyström, Kristina / Abrantes, Joana / Lopes, Ana Margarida / Le Moullac-Vaidye, Béatrice / Marchandeau, Stéphane / Rocher, Jézabel / Ruvoën-Clouet, Nathalie / Esteves, Pedro J / Le Pendu, Jacques

PLoS pathogens

2015 Volume 11, Issue 4, Page(s) e1004759

Abstract: RHDV (rabbit hemorrhagic disease virus), a virulent calicivirus, causes high mortalities in European rabbit populations (Oryctolagus cuniculus). It uses α1,2fucosylated glycans, histo-blood group antigens (HBGAs), as attachment factors, with their ... ...

Abstract	RHDV (rabbit hemorrhagic disease virus), a virulent calicivirus, causes high mortalities in European rabbit populations (Oryctolagus cuniculus). It uses α1,2fucosylated glycans, histo-blood group antigens (HBGAs), as attachment factors, with their absence or low expression generating resistance to the disease. Synthesis of these glycans requires an α1,2fucosyltransferase. In mammals, there are three closely located α1,2fucosyltransferase genes rSec1, rFut2 and rFut1 that arose through two rounds of duplications. In most mammalian species, Sec1 has clearly become a pseudogene. Yet, in leporids, it does not suffer gross alterations, although we previously observed that rabbit Sec1 variants present either low or no activity. Still, a low activity rSec1 allele correlated with survival to an RHDV outbreak. We now confirm the association between the α1,2fucosyltransferase loci and survival. In addition, we show that rabbits express homogenous rFut1 and rFut2 levels in the small intestine. Comparison of rFut1 and rFut2 activity showed that type 2 A, B and H antigens recognized by RHDV strains were mainly synthesized by rFut1, and all rFut1 variants detected in wild animals were equally active. Interestingly, rSec1 RNA levels were highly variable between individuals and high expression was associated with low binding of RHDV strains to the mucosa. Co-transfection of rFut1 and rSec1 caused a decrease in rFut1-generated RHDV binding sites, indicating that in rabbits, the catalytically inactive rSec1 protein acts as a dominant-negative of rFut1. Consistent with neofunctionalization of Sec1 in leporids, gene conversion analysis showed extensive homogenization between Sec1 and Fut2 in leporids, at variance with its limited degree in other mammals. Gene conversion additionally involving Fut1 was also observed at the C-terminus. Thus, in leporids, unlike in most other mammals where it became extinct, Sec1 evolved a new function with a dominant-negative effect on rFut1, contributing to fucosylated glycan diversity, and allowing herd protection from pathogens such as RHDV.
MeSH term(s)	Animals ; Base Sequence ; Caliciviridae Infections/genetics ; Disease Resistance/genetics ; Fucosyltransferases/genetics ; Hemorrhagic Disease Virus, Rabbit/genetics ; Lagomorpha ; Molecular Sequence Data ; Polymerase Chain Reaction ; Polymorphism, Genetic ; Polysaccharides/genetics ; Rabbits ; Transfection
Chemical Substances	Polysaccharides ; Fucosyltransferases (EC 2.4.1.-)
Language	English
Publishing date	2015-04-15
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2205412-1
ISSN	1553-7374 ; 1553-7366
ISSN (online)	1553-7374
ISSN	1553-7366
DOI	10.1371/journal.ppat.1004759
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