Immunocytochemical Assessment of ACE2 and TMPRSS2 in Nasopharyngeal Swabs from SARS-CoV-2 Patients.

ACE2 Procleix\textregistered{} assay SARS-CoV-2 TMPRSS2 cytology immunohistochemical liquid-based nasopharynx swab universal transport medium

Journal

Frontiers in bioscience (Landmark edition)
ISSN: 2768-6698
Titre abrégé: Front Biosci (Landmark Ed)
Pays: Singapore
ID NLM: 101612996

Informations de publication

Date de publication:
11 07 2022
Historique:
received: 01 04 2022
revised: 27 06 2022
accepted: 06 07 2022
entrez: 22 7 2022
pubmed: 23 7 2022
medline: 26 7 2022
Statut: ppublish

Résumé

SARS-CoV-2 is a positive-sense single-stranded RNA virus. It is enveloped by four structural proteins. The entry of the virus into the host cells is mediated by spike protein binding to the angiotensin converting enzyme 2 (ACE2) and proteolytic cleavage by transmembrane protease serine 2 (TMPRSS2). In this study, we analyzed the expression of the ACE2 receptor and TMPRSS2 in cases under investigation for SARS-CoV-2 infection. The study was carried out using the viral transport medium of consecutive nasopharyngeal swabs from 300 people under examination for SARS-CoV-2 infection. All samples underwent the SARS-CoV-2 transcriptase-mediated amplification assay (Procleix® SARS-CoV-2) to detect the virus. Immunocytochemistry was used in each sample to detect the presence of the SARS-CoV-2 nucleoprotein, the ACE2 receptor, and TMPRSS2. An immunocytochemical study with monoclonal antibody against SARS-CoV-2 viral nucleoprotein showed positivity in squamous cells. ACE2 were not detected in the squamous cells obtained from the nasopharyngeal samples. SARS-CoV-2 predominantly localizes to squamous cells in cytology samples of patients with positive transcriptase-mediated amplification SARS-CoV-2 assay results. The immunocytochemical negativity for ACE2 evidenced in the present study could be related to the cellular heterogeneity present in the nasopharyngeal smear samples and could be related to variations at the genomic level. Our results suggest that SARS-CoV-2 might be present in the nasopharyngeal region because viral cell junctions are weaker. This facilitates viral concentration, infective capacity and migration to specific organs, where SARS-CoV-2 infects target cells by binding to their receptors and then entering.

Sections du résumé

BACKGROUND
SARS-CoV-2 is a positive-sense single-stranded RNA virus. It is enveloped by four structural proteins. The entry of the virus into the host cells is mediated by spike protein binding to the angiotensin converting enzyme 2 (ACE2) and proteolytic cleavage by transmembrane protease serine 2 (TMPRSS2). In this study, we analyzed the expression of the ACE2 receptor and TMPRSS2 in cases under investigation for SARS-CoV-2 infection.
METHODS
The study was carried out using the viral transport medium of consecutive nasopharyngeal swabs from 300 people under examination for SARS-CoV-2 infection. All samples underwent the SARS-CoV-2 transcriptase-mediated amplification assay (Procleix® SARS-CoV-2) to detect the virus. Immunocytochemistry was used in each sample to detect the presence of the SARS-CoV-2 nucleoprotein, the ACE2 receptor, and TMPRSS2.
RESULTS
An immunocytochemical study with monoclonal antibody against SARS-CoV-2 viral nucleoprotein showed positivity in squamous cells. ACE2 were not detected in the squamous cells obtained from the nasopharyngeal samples.
CONCLUSIONS
SARS-CoV-2 predominantly localizes to squamous cells in cytology samples of patients with positive transcriptase-mediated amplification SARS-CoV-2 assay results. The immunocytochemical negativity for ACE2 evidenced in the present study could be related to the cellular heterogeneity present in the nasopharyngeal smear samples and could be related to variations at the genomic level. Our results suggest that SARS-CoV-2 might be present in the nasopharyngeal region because viral cell junctions are weaker. This facilitates viral concentration, infective capacity and migration to specific organs, where SARS-CoV-2 infects target cells by binding to their receptors and then entering.

Identifiants

pubmed: 35866407
pii: S2768-6701(22)00583-4
doi: 10.31083/j.fbl2707217
doi:

Substances chimiques

Angiotensin-Converting Enzyme 2 EC 3.4.17.23
Serine Endopeptidases EC 3.4.21.-
TMPRSS2 protein, human EC 3.4.21.-

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

217

Informations de copyright

© 2022 The Author(s). Published by IMR Press.

Déclaration de conflit d'intérêts

The authors declare no conflict of interest.

Auteurs

Karla Beatríz Peña (KB)

Pathology Molecular Unit, Department of Pathology, Sant Joan University Hospital, Pere Virgili Health Research Institute, Faculty of Medicine, Rovira and Virgili University, 43204 Reus (Tarragona), Spain.

Josep Gumà (J)

Department of Oncology, Sant Joan University Hospital, Pere Virgili Health Research Institute, Faculty of Medicine, Rovira and Virgili University, 43204 Reus (Tarragona), Spain.

Carmen Guilarte (C)

Pathology Molecular Unit, Department of Pathology, Sant Joan University Hospital, Pere Virgili Health Research Institute, Faculty of Medicine, Rovira and Virgili University, 43204 Reus (Tarragona), Spain.

Lola Delamo (L)

Department of Oncology, Sant Joan University Hospital, Pere Virgili Health Research Institute, Faculty of Medicine, Rovira and Virgili University, 43204 Reus (Tarragona), Spain.

Marc Grifol (M)

Department of Oncology, Sant Joan University Hospital, Pere Virgili Health Research Institute, Faculty of Medicine, Rovira and Virgili University, 43204 Reus (Tarragona), Spain.

Berta Pique (B)

Pathology Molecular Unit, Department of Pathology, Sant Joan University Hospital, Pere Virgili Health Research Institute, Faculty of Medicine, Rovira and Virgili University, 43204 Reus (Tarragona), Spain.

Anna Hernandez (A)

Pathology Molecular Unit, Department of Pathology, Sant Joan University Hospital, Pere Virgili Health Research Institute, Faculty of Medicine, Rovira and Virgili University, 43204 Reus (Tarragona), Spain.

Helena Casteñé (H)

Reserca Biomedical Unit, Sant Joan University Hospital, Pere Virgili Health Research Institute, Faculty of Medicine, Rovira and Virgili University, 43202 Reus (Tarragona), Spain.

Francesc Riu (F)

Pathology Molecular Unit, Department of Pathology, Sant Joan University Hospital, Pere Virgili Health Research Institute, Faculty of Medicine, Rovira and Virgili University, 43204 Reus (Tarragona), Spain.

David Parada (D)

Pathology Molecular Unit, Department of Pathology, Sant Joan University Hospital, Pere Virgili Health Research Institute, Faculty of Medicine, Rovira and Virgili University, 43204 Reus (Tarragona), Spain.

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Classifications MeSH