The life cycle and enigmatic egress of coronaviruses

Prydz, Kristian; Saraste, Jaakko

doi:10.1111/mmi.14907

Cited by 16 publications

(12 citation statements)

References 149 publications

(191 reference statements)

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“…Indeed, the intermediate compartment (IC) not only is known to be a linker between the ER and the Golgi compartments but is also implicated in Golgi-independent transport routes to the plasma membrane. This alternative exocytic process has been described to increase the yield and the release of active viral particles ( Prydz and Saraste, 2022 ).…”

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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“…Based on their motor-dependent movements along cytoskeletal tracks, either actin filaments or microtubules (MTs), they can assume a more widespread distribution in certain cells, or accumulate at the cell center in others, establishing the pericentrosomal endocytic recycling compartment (ERC) (Maxfield and McGraw 2004 ; Misaki et al. 2010 ; Naslavsky and Caplan 2018 ). Moreover, a subpopulation of REs has recently been shown to closely associate with the trans -side of the Golgi stacks (Fujii et al.…”

Section: Resultsmentioning

confidence: 99%

Evidence for the role of Rab11-positive recycling endosomes as intermediates in coronavirus egress from epithelial cells

Saraste

Enyioko

Dale

et al. 2022

Histochem Cell Biol

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After their assembly by budding into the lumen of the intermediate compartment (IC) at the endoplasmic reticulum (ER)–Golgi interface, coronaviruses (CoVs) are released from their host cells following a pathway that remains poorly understood. The traditional view that CoV exit occurs via the constitutive secretory route has recently been questioned by studies suggesting that this process involves unconventional secretion. Here, using the avian infectious bronchitis virus (IBV) as a well-established model virus, we have applied confocal microscopy to investigate the pathway of CoV egress from epithelial Vero cells. We report a novel effect of IBV infection on cellular endomembranes, namely, the compaction of the pericentrosomal endocytic recycling compartment (ERC) defined by the GTPase Rab11, which coincides with the previously described Golgi fragmentation, as well as virus release. Despite Golgi disassembly, the IC elements containing the major IBV membrane protein (M)—which mostly associates with newly formed virus particles—maintain their close spatial connection with the Rab11-positive endocytic recycling system. Moreover, partial colocalization of the M protein with Rab11 was observed, whereas M displayed negligible overlap with LAMP-1, indicating that IBV egress does not occur via late endosomes or lysosomes. Synchronization of virus release using temperature-shift protocols was accompanied by increased colocalization of M and Rab11 in vesicular and vacuolar structures in the pericentrosomal region and at the cell periphery, most likely representing IBV-containing transport carriers. In conclusion, these results add CoVs to the growing list of viruses exploiting the endocytic recycling apparatus defined by Rab11 for their assembly and/or release.

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“…SDC-mediated cellular entry occurs mainly through clathrin-independent routes involving lipid rafts [ 52 ]. Ligands entering the cells via clathrin-independent SDC-mediated pathways can bypass lysosomal degradation [ 52 , 53 , 54 , 55 , 56 ]. Thus, by avoiding lysosomes, the SDC-mediated internalization of SARS-CoV-2 can paradoxically inhibit the formation of new viruses egressing from lysosomes.…”

Section: Discussionmentioning

confidence: 99%

Biodistribution and Cellular Internalization of Inactivated SARS-CoV-2 in Wild-Type Mice

Hudák¹,

Morgan²,

Bačovský

et al. 2022

IJMS

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Despite the growing list of identified SARS-CoV-2 receptors, the human angiotensin-converting enzyme 2 (ACE2) is still viewed as the main cell entry receptor mediating SARS-CoV-2 internalization. It has been reported that wild-type mice, like other rodent species of the Muridae family, cannot be infected with SARS-CoV-2 due to differences in their ACE2 receptors. On the other hand, the consensus heparin-binding motif of SARS-CoV-2′s spike protein, PRRAR, enables the attachment to rodent heparan sulfate proteoglycans (HSPGs), including syndecans, a transmembrane HSPG family with a well-established role in clathrin- and caveolin-independent endocytosis. As mammalian syndecans possess a relatively conserved structure, we analyzed the cellular uptake of inactivated SARS-CoV-2 particles in in vitro and in vivo mice models. Cellular studies revealed efficient uptake into murine cell lines with established syndecan-4 expression. After intravenous administration, inactivated SARS-CoV-2 was taken up by several organs in vivo and could also be detected in the brain. Internalized by various tissues, inactivated SARS-CoV-2 raised tissue TNF-α levels, especially in the heart, reflecting the onset of inflammation. Our studies on in vitro and in vivo mice models thus shed light on unknown details of SARS-CoV-2 internalization and help broaden the understanding of the molecular interactions of SARS-CoV-2.

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The life cycle and enigmatic egress of coronaviruses

Cited by 16 publications

References 149 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

Evidence for the role of Rab11-positive recycling endosomes as intermediates in coronavirus egress from epithelial cells

Biodistribution and Cellular Internalization of Inactivated SARS-CoV-2 in Wild-Type Mice

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