3rd Glyco Morning Event with Jacques Le Pendu

on the September 7, 2017

At 10:00am
Jacques Le Pendu, from Inserm Nantes, is the third invited speaker participating to the Glyco Morning Events. The event will take place on Thursday 7 September at Cermav.
The third Glyco Morning event will take place at Cermav on Thursday 7 September from 10 to 12. The invited speaker is Jacques Le Pendu, from Inserm Nantes, who will give a talk on the “Role of Histo-blood group antigens (HBGAs) in enteric virus infection”. Two young glycoscientists from Glyco@Alps, Silvia Achilli (IBS° and David Goyard (DCM) will kick off the event with short talks.

10:00 Young glycoscientists talks
10:40 Coffee break and discussions
11:00 Invited speaker: Jacques Le Pendu

Invited speaker

Role of Histo-blood group antigens (HBGAs) in enteric virus infection
Jacques Le Pendu, Centre de Recherche en Cancérologie Nantes-Angers, Inserm Nantes

Human caliciviruses, more specifically, noroviruses (NoVs), and type A rotaviruses (RVAs) represent the most common cause of gastroenteritis. Despite their complete lack of phylogenetic relationship, strains of these two virus families present similar recognition properties for glycans [1]. Their common HBGA-binding specificities suggest shared molecular mechanisms of infection. Moreover, either volunteers’ studies and/or analyses of outbreaks demonstrated that for both NoVs and RVAs, the HBGA polymorphism restricts infection to individuals presenting matching HBGA motifs [2,3]. Thus, a given strain appears to infect (or generate symptoms) a subgroup of the population only, suggesting a co-evolution between humans and both NoVs and RVAs that led to a trade-off where the human population is partly protected, whilst the viruses circulation is maintained [4]. This co-evolution could be documented using an animal model studied in naturo, taking profit of the relationship between wild rabbits and RHDV, a virus of the calicivirus family, that shares its HBGA binding properties with NoVs and RVAs [5]. I called « Herd Innate Protection » the partial protection afforded by the HBGAs polymorphism. This concept may bear important implications for the development of vaccines. In addition, blocking glycan-binding could provide a common preventive or therapeutic approach.

1. Tan M, Jiang X. Histo-blood gorup antigens: a common nich for norovirus and rotavirus. Expert Rev Mol Med. 2014;16:e5.
2. Ruvöen-Clouet N, Belliot G, Le Pendu J. Noroviruses and histo-blood groups: the impact of common host genetic polymorphisms on virus transmission and evolution. Rev Med Virol. 2013;23:355-66.
3. Imbert-Marcille B-M, Barbé L, Dupé M, Le Moullac-Vaidye B, Besse B, Peltier C, et al. A FUT2 gene common polymorphism determines resistance to rotavirus A of the P[8] genotype. J Infect Dis. 2013;209:1227-30.
4. Le Pendu J, Nystrom K, Ruvoen-Clouet N. Host-pathogen co-evolution and glycan interactions. Curr Opin Virol. 2014;7:88-94. 5. Nyström K, Le Gall-Reculé G, Grassi P, Abrantes J, Ruvoën-Clouet N, Le Moullac-Vaidye B, et al. Histo-Blood Group Antigens act as attachment factors of Rabbit Hemorrhagic Disease Virus infection in a virus strain-dependent manner. PLoS Pathogens. 2011;7(8):e1002188 and Lopes et al submitted.

Young scientists talks

Oriented SPR surface to study Clusters Targeting C-type Lectin Receptors: towards tools for an anticancer immune response activation
Silvia Achilli, Institut de Biologie Structurale

The adaptive immune system is a complex system we try to study with well-defined synthetic single molecules. In this work we quantified the interaction between C-type Lectin Receptors and mannose clusters through SPR direct approach.

Synthesis of High Affinity Glycoclusters and Binding Studies with Bacterial Lectins
David Goyard, Département de Chimie Moléculaire

Many microorganisms use lectins as adhesins to interact with host glycoconjugates and to trigger the first step of infection. Among those, several opportunistic pathogens responsible for lung infection produce soluble lectins with high affinity for glycans present on host tissues. In order to reach those high affinities lectins often adopt multimeric architectures, presenting several sites that bind clusters of carbohydrate ligands. The resulting interaction, being a combination of simultaneous binding events, is significantly stronger and is known as the “glycoside cluster effect”. Capitalizing on this effect, it was recently demonstrated that synthetic molecules that can compete with natural ligands of these proteins can potentially prevent cell adhesion and biofilm formation. Therapeutic effects have indeed been observed with fucose- and galactose-based structures against Pseudomonas aeruginosa, which highlights the potency of this new lectin-directed anti-adhesion strategy against pathogenic bacteria.

Published on August 29, 2017

Practical informations


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