Importance of viral late domains in budding and release of enveloped RNA viruses

Welker, Lisa; Paillart, Jean-Christophe; Bernacchi, Serena

doi:10.3390/v13081559

Cited by 36Cellular transport and secretionVirology and Viral DiseasesHIV Research and Treatment

Importance of viral late domains in budding and release of enveloped RNA viruses

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Welker, Lisa, Paillart, Jean-Christophe, Bernacchi, Serena·2021·Viruses

DOI 10.3390/v13081559PMC PMC8402826

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Abstract

Late assembly (L) domains are conserved sequences that are necessary for the late steps of viral replication, acting like cellular adaptors to engage the ESCRT membrane fission machinery that promote virion release. These short sequences, whose mutation or deletion produce the accumulation of immature virions at the plasma membrane, were firstly identified within retroviral Gag precursors, and in a further step, also in structural proteins of many other enveloped RNA viruses including arenaviruses, filoviruses, rhabdoviruses, reoviruses, and paramyxoviruses. Three classes of L domains have been identified thus far (PT/SAP, YPXnL/LXXLF, and PPxY), even if it has recently been suggested that other motifs could act as L domains. Here, we summarize the current state of knowledge of the different types of L domains and their cellular partners in the budding events of RNA viruses, with a particular focus on retroviruses.

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L domains are short, 4-6 amino acid domains that act like cellular adaptor proteins, ensuring membrane scission and virion separation from host cell membranes.
“These short, 4–6 amino acid domains act like cellular adaptor proteins, ensuring membrane scission and virion separation from the host cell membranes”
From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Welker et al. 2021
The Introduction describes L domains as motifs that act like cellular adaptor proteins, and Section 2 links these short sequences to virion separation from the cell membrane. The copy identifies several four-residue motifs, but it does not establish that L domains are uniformly 4–6 amino acids long; one listed motif, YPXnL, has variable length. No page numbers are available in the copy. (LLM, conf=0.78)
Experimental — accuracy not yet measured
Retroviral Gag recruits ESCRT machinery via conserved motifs termed late assembly domains (L domains).
“Retroviral Gag has been implicated in recruiting ESCRT machinery via conserved motifs, termed late assembly domains (“L” domains).”
From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Welker et al. 2021

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Authors: Welker, L., Paillart, J.-C., & Bernacchi, S.
Affiliations: Centre National de la Recherche Scientifique (FR)
Corresponding author: Bernacchi, Serena
ORCID: Welker, Lisa
Paillart, Jean-Christophe
Bernacchi, Serena
Venue: Viruses
Publisher: MDPI AG
Published: 2021-08-06
Volume: 13
Issue: 8
Pages: 1559
ISSN: 1999-4915 (ISSN-L)
DOI: 10.3390/v13081559
PMC: PMC8402826
OpenAlex: W3187623180
Cited by: 36
References: 180
Citations by year: 2026: 5 · 2025: 8 · 2024: 7 · 2023: 10 · 2022: 4 · 2021: 2
FWCI: 0.73
Type: journal article
Language: en
Open access: gold
doi.org
Licence: cc-by
creativecommons.org/licenses/by/4.0/ (vor)
Locations: Viruses (publishedVersion, cc-by)
PubMed Central (publishedVersion, cc-by)
PubMed (publishedVersion)
HAL (submittedVersion, other-oa)
DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders: Agence Nationale de Recherches sur le Sida et les Hépatites Virales (Appel à Projets 2020-1)
IdEx (2020-202)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Health Sciences › Medicine › Epidemiology › Virology and Viral Diseases
Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
Keywords: viral budding, virion release, ESCRT machinery, membrane fission, enveloped RNA viruses, retroviruses, Gag, PPxY motif, immature virions, arenaviruses, filoviruses, rhabdovirus, reovirus, paramyxovirus
MeSH terms: Humans, Protein Binding, RNA Viruses, Virion, Virus Replication, Virus Assembly, Ubiquitination, Endosomal Sorting Complexes Required for Transport, Virus Release

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Importance of viral late domains in budding and release of enveloped RNA viruses

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