The Lectin ERGIC-53 Goes Viral

Pasquato, Antonella; Kunz, Stefan

doi:10.1016/j.chom.2013.10.014

Cited by 2 publications

(3 citation statements)

References 10 publications

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“…It has been demonstrated that the loss of ERGIC-53 or its activity leads to a defective assembly of virions that are unable to attach host cells. Interestingly, ERGIC-53 specifically interacts with class I viral fusion glycoproteins which also include the SARS-CoV-2 Spike protein ( Pasquato and Kunz, 2013 ). In the NCM460D cell line, much more than in the others, we assist to a high enrichment in Rabs proteins involved in the exocytic pathway such as RAB1A and RAB1B .…”

Section: Resultsmentioning

confidence: 99%

Spike S1 domain interactome in non-pulmonary systems: A role beyond the receptor recognition

Iacobucci

Monaco

Canè

et al. 2022

Front. Mol. Biosci.

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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.

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Section: Resultsmentioning

confidence: 99%

Spike S1 domain interactome in non-pulmonary systems: A role beyond the receptor recognition

Iacobucci

Monaco

Canè

et al. 2022

Front. Mol. Biosci.

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“…Viral propagation is enabled when the targets such as stress granule (SG)‐associated Ras GTPase‐activating protein‐binding protein 1 (G3BP1) and heterogeneous nuclear ribonucleoproteins (hnRNPs) get relocated in cytoplasmic punctuated structures and further gets attached with NP 42 . GP is delivered to budding sites via the ER‐Golgi Pathway with the help of host factors such as ADP‐ribosylation factor 1, a GTP‐binding protein, which operates in the ER–Golgi complex, and ER–Golgi Intermediate Compartment 53 kDa protein (ERGIC‐53) 43 . The profile of the lipid on the plasma membrane determines the acceptance of glycoprotein into virions.…”

Section: Nature Of Infectious Agents (Structural and Molecular)mentioning

confidence: 99%

“…42 protein (ERGIC-53). 43 The profile of the lipid on the plasma membrane determines the acceptance of glycoprotein into virions. It is affected by lipid rafts and cholesterol content.…”

Section: Nature Of Infectious Agents (Structural and Molecular)mentioning

confidence: 99%

Recent developments on Junin virus, a causative agent for Argentine haemorrhagic fever

Kumar

Yadav

Singh

et al. 2023

Reviews in Medical Virology

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Junin virus consists of ribonucleic acid as the genome and is responsible for a rapidly changing tendency of the virus. The virus is accountable for ailments in the human body and causes Argentine Haemorrhagic Fever (AHF). The infection is may be transmitted through contact between an infected animal/host and a person, and later between person to person. Prevention of outbreaks of AHF in humans can be a tough practice, as their occurrence is infrequent and unpredictable. In this review, recent information from the past 5 years available on the Junin virus including the risk of its emergence, infectious agents, its pathogenesis in humans, available diagnostic and therapeutic approaches, and disease management has been summarised. Altogether, this article would be highly significant in understanding the mechanistic basis behind virus interaction and other processes during the life cycle.Currently, no specific therapeutic options are available to treat the Junin virus infection. The information covered in this review could be important for finding possible treatment options for Junin virus infections.

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The Lectin ERGIC-53 Goes Viral

Cited by 2 publications

References 10 publications

Spike S1 domain interactome in non-pulmonary systems: A role beyond the receptor recognition

Spike S1 domain interactome in non-pulmonary systems: A role beyond the receptor recognition

Recent developments on Junin virus, a causative agent for Argentine haemorrhagic fever

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