title: Glycans in Infectious Diseases. A Molecular Recognition Perspective.
abstract: BACKGROUND
  From the simplest bacteria to the highest complex mammals, including humans, every single cell is covered by a dense coat of glycans. Glycans are involved in almost every biological process that takes place in our body, playing a central role in the communication between cells and their environment. Glycans are also involved in infectious diseases, which arise from the specific interaction between glycans of the pathogen cell coat and specific receptors on the host cell or vice versa.
  
  
  OBJECTIVE
  The understanding of the mechanisms governing these specific carbohydrateprotein interactions, at atomic and molecular levels, is crucial to develop new drugs able to block the infection and to avoid the disease.
  
  
  METHODS
  Recent advances in biophysical techniques allow for a complete picture of the hostpathogen infection event, unveiling the key aspects of the molecular interaction and, thus, providing an opportunity to interfere with it.
  
  
  CONCLUSIONS
  In this general review, we discuss some recent contributions, providing a summary of what we consider the most innovative and inspiring research lines to the field.
authors.affiliation: CIC bioGUNE, Bizkaia Technology Park, Building 801A, 48170 Derio, Spain.
authors.forename: Luca
authors.initials: L
authors.lastname: Unione
authors.affiliation: CIC bioGUNE, Bizkaia Technology Park, Building 801A, 48170 Derio, Spain.
authors.forename: Ana
authors.initials: A
authors.lastname: Gimeno
authors.affiliation: CIC bioGUNE, Bizkaia Technology Park, Building 801A, 48170 Derio, Spain.
authors.forename: Pablo
authors.initials: P
authors.lastname: Valverde
authors.affiliation: CIC bioGUNE, Bizkaia Technology Park, Building 801A, 48170 Derio, Spain.|Departament of Organic Chemistry II, Faculty of Science & Technology, University of the Basque Country, 48940 Leioa, Bizkaia, Spain.
authors.forename: Ilaria
authors.initials: I
authors.lastname: Calloni
authors.affiliation: CIC bioGUNE, Bizkaia Technology Park, Building 801A, 48170 Derio, Spain.|Departament of Organic Chemistry II, Faculty of Science & Technology, University of the Basque Country, 48940 Leioa, Bizkaia, Spain.|UCIBIO, REQUIMTE, Departamento de Quimica, Faculdade de Ciencias e Tecnologia, Universidade Nova de Lisboa, 2829-516, Caparica, Portugal.
authors.forename: Helena
authors.initials: H
authors.lastname: Coelho
authors.affiliation: CIC bioGUNE, Bizkaia Technology Park, Building 801A, 48170 Derio, Spain.|Dipartimento di Chimica "Ugo Schiff", Università degli Studi di Firenze, 50019 Sesto Fiorentino (FI), Italy.
authors.forename: Stefania
authors.initials: S
authors.lastname: Mirabella
authors.affiliation: CIC bioGUNE, Bizkaia Technology Park, Building 801A, 48170 Derio, Spain.
authors.forename: Ana
authors.initials: A
authors.lastname: Poveda
authors.affiliation: CIC bioGUNE, Bizkaia Technology Park, Building 801A, 48170 Derio, Spain.
authors.forename: Ana
authors.initials: A
authors.lastname: Arda
authors.affiliation: CIC bioGUNE, Bizkaia Technology Park, Building 801A, 48170 Derio, Spain.|Ikerbasque, Basque Foundation for Science, Maria Diaz de Haro 13, 48009 Bilbao, Spain.|Departament of Organic Chemistry II, Faculty of Science & Technology, University of the Basque Country, 48940 Leioa, Bizkaia, Spain.
authors.forename: Jesus
authors.initials: J
authors.lastname: Jimenez-Barbero
mesh_terms: D000818:Animals; D015703:Antigens, CD / Q000737:chemistry / Q000378:metabolism; D000998:Antiviral Agents / Q000737:chemistry / Q000378:metabolism; D001422:Bacterial Adhesion; D001424:Bacterial Infections / Q000378:metabolism / Q000473:pathology; D003141:Communicable Diseases / Q000378:metabolism / Q000473:pathology*; D006801:Humans; D009980:Influenza A virus / Q000201:enzymology; D037181:Lectins, C-Type / Q000737:chemistry / Q000378:metabolism; D037241:Mannose-Binding Lectins / Q000737:chemistry / Q000378:metabolism; D009439:Neuraminidase / Q000037:antagonists & inhibitors / Q000378:metabolism; D011134:Polysaccharides / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D051197:Toll-Like Receptor 4 / Q000737:chemistry / Q000378:metabolism; D014777:Virus Diseases / Q000378:metabolism / Q000473:pathology
chemical_list: D015703:Antigens, CD; D000998:Antiviral Agents; C121916:CD207 protein, human; D037181:Lectins, C-Type; D037241:Mannose-Binding Lectins; D011134:Polysaccharides; D051197:Toll-Like Receptor 4; D009439:Neuraminidase
keywords: Glycans; NMR; X-ray; bacterial infection; lectin; molecular recognition; viral infection.