B⁰AT1 Amino Acid Transporter Complexed With SARS-CoV-2 Receptor ACE2 Forms a Heterodimer Functional Unit: In Situ Conformation Using Radiation Inactivation Analysis.

ABSTRACT: The SARS-CoV-2 receptor, angiotensin-converting enzyme-2 (ACE2), is expressed at levels of greatest magnitude in the small intestine as compared with all other human tissues. Enterocyte ACE2 is coexpressed as the apical membrane trafficking partner obligatory for expression and activity of the B⁰AT1 sodium-dependent neutral amino acid transporter. These components are assembled as an [ACE2:B⁰AT1]₂ dimer-of-heterodimers quaternary complex that putatively steers SARS-CoV-2 tropism in the gastrointestinal (GI) tract. GI clinical symptomology is reported in about half of COVID-19 patients, and can be accompanied by gut shedding of virion particles. We hypothesized that within this 4-mer structural complex, each [ACE2:B⁰AT1] heterodimer pair constitut

SUBMITTER: Stevens BR 

PROVIDER: S-EPMC8194517 | biostudies-literature | 2021

REPOSITORIES: biostudies-literature