About: Novel ACE2-Independent Carbohydrate-Binding of SARS-CoV-2 Spike Protein to Host Lectins and Lung Microbiota

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About: Novel ACE2-Independent Carbohydrate-Binding of SARS-CoV-2 Spike Protein to Host Lectins and Lung Microbiota Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Novel ACE2-Independent Carbohydrate-Binding of SARS-CoV-2 Spike Protein to Host Lectins and Lung Microbiota
Creator	Molinaro, Antonio Li, R Van Kooyk, Yvette Bruijns, Sven Chiodo, Fabrizio Garcia-Rivera, Dagmar Lorenzo, Flaviana Rodriguez, Ernesto Silipo, Alba Valdes-Balbin, Yury Verez-Bencomo, Vicente
Source	BioRxiv
abstract	The immediate call for translational research in the field of coronavirus disease (COVID-19) pandemic, needs new and unexplored angles to support and contribute to this important worldwide health problem. The aim of this study is to better understand the pathogenic mechanisms underlying COVID-19, deciphering the carbohydrate-mediated interactions of the SARS-CoV-2 spike protein. We studied the carbohydrate-binding receptors that could be important for viral entry and for immune-modulatory responses, and we studied the interactions of the spike protein with the host lung microbiota. Exploring solid-phase immunoassays, we evaluated the interactions between the SARS-CoV-2 spike protein and a library of 12 different human carbohydrate-binding proteins (C-type lectins and Siglecs) involved in binding, triggering and modulation of innate and adaptive immune-responses. We revealed a specific binding of the SARS-CoV-2 spike protein to the receptors DC-SIGN, MGL, Siglec-9 and Siglec-10 that are all expressed on myeloid immune cells. In addition, because the lung microbiota can promote or modulate viral infection, we studied the interactions between the SARS-CoV-2 spike protein and a library of Streptococcus pneumoniae capsular polysaccharides, as well as other bacterial glyco-conjugates. We show specific binding of the spike protein to different S. pneumoniae capsular polysaccharides (serotypes 19F and 23F but not to serotype 14). Moreover we demonstrated a specific binding of SARS-CoV-2 spike protein to the lipopolysaccharide from the opportunistic human pathogen Pseudomonas aeruginosa, one of the leading cause of acute nosocomial infections and pneumonia. Interestingly, we identified rhamnosylated epitopes as one of the discriminating structures in lung microbiota to bind SARS-CoV-2 spike protein. In conclusion, we revealed novel ACE2-independent carbohydrate-mediated interactions with immune modulating lectins expressed on myeloid cells, as well as host lung microbiota glyco-conjugates. Our results identified new molecular pathways using host lectins and signalling, that may contribute to viral infection and subsequent immune exacerbation. Moreover we identified specific rhamnosylated epitopes in lung microbiota to bind SARS-CoV-2, providing a hypothetical link between the presence of specific lung microbiota and SARS-CoV-2 infection and severity.
has issue date	2020-05-14(xsd:dateTime)
bibo:doi	10.1101/2020.05.13.092478
has license	biorxiv
sha1sum (hex)	a731269a16e4382d1d8e962e5ed44aaa4855c70d
schema:url	https://doi.org/10.1101/2020.05.13.092478
resource representing a document's title	Novel ACE2-Independent Carbohydrate-Binding of SARS-CoV-2 Spike Protein to Host Lectins and Lung Microbiota
schema:publication	bioRxiv
resource representing a document's body	covid:a731269a16e4382d1d8e962e5ed44aaa4855c70d#body_text
is schema:about of	named entity 'spike' named entity 'identified' named entity 'microbiota' named entity 'adaptive' named entity 'signalling' named entity 'identified' named entity 'revealed' named entity 'addition' named entity 'triggering' covid:arg/a731269a16e4382d1d8e962e5ed44aaa4855c70d named entity 'epitopes' named entity 'bind' named entity 'protein' named entity 'pathogenic' named entity 'SARS-CoV-2' named entity 'specific' named entity 'myeloid' named entity 'DC-SIGN' named entity 'myeloid' named entity 'involved' named entity 'C-type' named entity 'leading' named entity 'interactions' named entity 'COVID-19' named entity 'microbiota' named entity 'promote' named entity 'discriminating' named entity 'coronavirus' named entity 'binding' named entity 'serotypes' named entity 'carbohydrate' named entity 'nosocomial infections' named entity 'lung' named entity 'SARS-CoV-2' named entity 'spike protein' named entity 'epitopes' named entity 'S. pneumoniae' named entity 'myeloid cells' named entity 'translational research' named entity 'Streptococcus pneumoniae' named entity 'spike protein' named entity 'spike protein' named entity 'SARS-CoV-2' named entity 'ACE2' named entity 'COVID' named entity 'SARS-CoV-2' named entity 'COVID' named entity 'microbiota' named entity 'pneumonia' named entity 'spike protein' named entity 'Spike Protein' named entity 'ACE2' named entity 'SARS-CoV-2' named entity 'HEK293' named entity 'immunoassay' named entity 'co-evolved' named entity 'dendritic cells' named entity 'inhibit viral entry' named entity 'pathogens' named entity 'glycans' named entity 'sialylated' named entity 'MERS' named entity 'evolutionary pressure' named entity 'Ebolavirus' named entity 'DC-SIGN' named entity 'SARS-CoV-2' named entity 'viral infections' named entity 'ELISA assay' named entity 'DC-SIGN' named entity 'lectins' named entity 'SARS-CoV-2' named entity '293 cells' named entity 'galactose' named entity 'N165'

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