Arthropod Ectoparasites Have Potential to Bind SARS-CoV-2 via ACE.


Journal

Viruses
ISSN: 1999-4915
Titre abrégé: Viruses
Pays: Switzerland
ID NLM: 101509722

Informations de publication

Date de publication:
19 04 2021
Historique:
received: 02 04 2021
revised: 16 04 2021
accepted: 16 04 2021
entrez: 30 4 2021
pubmed: 1 5 2021
medline: 7 5 2021
Statut: epublish

Résumé

Coronavirus-like organisms have been previously identified in Arthropod ectoparasites (such as ticks and unfed cat flea). Yet, the question regarding the possible role of these arthropods as SARS-CoV-2 passive/biological transmission vectors is still poorly explored. In this study, we performed in silico structural and binding energy calculations to assess the risks associated with possible ectoparasite transmission. We found sufficient similarity between ectoparasite ACE and human ACE2 protein sequences to build good quality 3D-models of the SARS-CoV-2 Spike:ACE complex to assess the impacts of ectoparasite mutations on complex stability. For several species (e.g., water flea, deer tick, body louse), our analyses showed no significant destabilisation of the SARS-CoV-2 Spike:ACE complex, suggesting these species would bind the viral Spike protein. Our structural analyses also provide structural rationale for interactions between the viral Spike and the ectoparasite ACE proteins. Although we do not have experimental evidence of infection in these ectoparasites, the predicted stability of the complex suggests this is possible, raising concerns of a possible role in passive transmission of the virus to their human hosts.

Identifiants

pubmed: 33921873
pii: v13040708
doi: 10.3390/v13040708
pmc: PMC8073597
pii:
doi:

Substances chimiques

Arthropod Proteins 0
Spike Glycoprotein, Coronavirus 0
spike protein, SARS-CoV-2 0
Peptidyl-Dipeptidase A EC 3.4.15.1
ACE2 protein, human EC 3.4.17.23
Angiotensin-Converting Enzyme 2 EC 3.4.17.23

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

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Auteurs

Su Datt Lam (SD)

Institute of Structural and Molecular Biology, UCL, Darwin Building, Gower Street, London WC1E 6BT, UK.
Department of Applied Physics, Faculty of Science and Technology, Universiti Kebangsaan Malaysia, Bangi 43600, Selangor, Malaysia.

Paul Ashford (P)

Institute of Structural and Molecular Biology, UCL, Darwin Building, Gower Street, London WC1E 6BT, UK.

Sandra Díaz-Sánchez (S)

SaBio, Instituto de Investigación en Recursos Cinegéticos IREC-CSIC-UCLM-JCCM, Ronda de Toledo s/n, 13005 Ciudad Real, Spain.

Margarita Villar (M)

SaBio, Instituto de Investigación en Recursos Cinegéticos IREC-CSIC-UCLM-JCCM, Ronda de Toledo s/n, 13005 Ciudad Real, Spain.
Regional Centre for Biomedical Research (CRIB), Biochemistry Section, Faculty of Science and Chemical Technologies, University of Castilla-La Mancha, 13071 Ciudad Real, Spain.

Christian Gortázar (C)

SaBio, Instituto de Investigación en Recursos Cinegéticos IREC-CSIC-UCLM-JCCM, Ronda de Toledo s/n, 13005 Ciudad Real, Spain.

José de la Fuente (J)

SaBio, Instituto de Investigación en Recursos Cinegéticos IREC-CSIC-UCLM-JCCM, Ronda de Toledo s/n, 13005 Ciudad Real, Spain.
Center for Veterinary Health Sciences, Department of Veterinary Pathobiology, Oklahoma State University, Stillwater, OK 74078, USA.

Christine Orengo (C)

Institute of Structural and Molecular Biology, UCL, Darwin Building, Gower Street, London WC1E 6BT, UK.

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Classifications MeSH