PXD035709

PXD035709 is an original dataset announced via ProteomeXchange.

Title	Spike S1 domain interactome in non-pulmonary systems: a role beyond the receptor recognition
Description	Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) causes Coronavirus Disease 2019 (COVID-19), which, since 2019 in China, has rapidly become a worldwide pandemic. The aggressiveness and global spread were enhanced by the many SARS-CoV-2 variants that have been isolated up to now. These mutations affect mostly the viral glycoprotein Spike (S), the capsid protein mainly involved in the early stages of viral entry processes, through the recognition of specific receptors on the host cell surface. In particular, the subunit S1 of the Spike glycoprotein contains the Receptor Binding Domain (RBD) and it is responsible for the interaction with the angiotensin-converting enzyme 2 (ACE2). Although ACE2 is the primary Spike host receptor currently studied, it has been demonstrated that SARS-CoV-2 is also able to infect cells expressing low levels of ACE2, indicating that the virus may have alternative receptors on the host cells. The identification of the alternative receptors can better elucidate the pathogenicity and the tropism of SARS-CoV-2. Therefore, we investigated the Spike S1 interactomes, starting from host membrane proteins of non-pulmonary cell lines, such as human kidney (HK-2), normal colon (NCM460D), and colorectal adenocarcinoma (Caco-2). We employed an affinity purification-mass spectrometry (AP-MS) to pull down, from the membrane protein extracts of all cell lines, the protein partners of the recombinant form of the Spike S1 domain. The purified interactors were identified by a shotgun proteomics approach. The lists of S1 potential interacting proteins were then clusterized according to cellular localization, biological processes, and pathways, highlighting new possible S1 intracellular functions, crucial not only for the entrance mechanisms but also for viral replication and propagation processes.
HostingRepository	PRIDE
AnnounceDate	2024-10-07
AnnouncementXML	Submission_2024-10-07_13:46:30.445.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	ilaria iacobucci
SpeciesList	scientific name: Homo sapiens (Human); NCBI TaxID: 9606;
ModificationList	(R)-5-oxo-1,4-tetrahydrothiazine-3-carboxylic acid; monohydroxylated residue; iodoacetamide derivatized residue
Instrument	LTQ

Revision	Datetime	Status	ChangeLog Entry
0	2022-08-02 01:42:19	ID requested
⏵ 1	2024-10-07 13:46:31	announced

Iacobucci I, Monaco V, Can, è L, Bibb, ò F, Cioffi V, Cozzolino F, Guarino A, Zollo M, Monti M, Spike S1 domain interactome in non-pulmonary systems: A role beyond the receptor recognition. Front Mol Biosci, 9():975570(2022) [pubmed]

10.3389/fmolb.2022.975570;

submitter keyword: AP-MS,SARS-CoV-2, proteomics, S1 domain, interactomics, host-virus interaction, COVID-19, Spike protein

Maria Monti
contact affiliation	Department of Chemical Sciences, University of Naples “Federico II”, Naples, Italy CEINGE Advanced Biotechnologies, Naples, Italy
contact email	montimar@unina.it
lab head
ilaria iacobucci
contact affiliation	Department of Chemical Sciences, University of Naples Federico II, Naples 80126, Italy CEINGE Advanced Biotechnologies, University of Naples Federico II, Naples 80145, Italy
contact email	iacobucci@ceinge.unina.it
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD035709
     1. Label: PRIDE project
     2. Name: Spike S1 domain interactome in non-pulmonary systems: a role beyond the receptor recognition