Structural Analysis of Merkel Cell Polyomavirus (MCPyV) Viral Capsid Protein 1 (VP1) in HIV-1 Infected Individuals.
A549 Cells
Adult
Aged
Amino Acid Substitution
Capsid Proteins
/ chemistry
Cross-Sectional Studies
Female
HIV Infections
/ blood
HIV-1
/ pathogenicity
Humans
Male
Merkel cell polyomavirus
/ genetics
Middle Aged
Models, Molecular
Plasma
/ virology
Polyomavirus Infections
/ blood
Protein Conformation
Protein Stability
Urine
/ virology
Virus Replication
Young Adult
A549 culture system
HIV+ individuals
Merkel cell polyomavirus (MCPyV)
amino-acids mutation
protein structural organization
viral protein 1 (VP1)
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
27 Oct 2020
27 Oct 2020
Historique:
received:
22
09
2020
revised:
20
10
2020
accepted:
24
10
2020
entrez:
30
10
2020
pubmed:
31
10
2020
medline:
4
3
2021
Statut:
epublish
Résumé
Merkel cell polyomavirus (MCPyV) viral protein 1 (VP1) is the capsid protein that mediates virus attachment to host cell receptors and is the major immune target. Given the limited data on MCPyV VP1 mutations, the VP1 genetic variability was examined in 100 plasma and 100 urine samples from 100 HIV+ individuals. Sequencing of VP1 DNA in 17 urine and 17 plasma specimens, simultaneously MCPyV DNA positive, revealed that 27 samples displayed sequences identical to VP1 of MCC350 strain. VP1 from two urine specimens had either Thr47Ser or Ile115Phe substitution, whereas VP1 of one plasma contained Asp69Val and Ser251Phe substitutions plus deletion (∆) of Tyr79. VP1 DNA in the remaining samples had mutations encoding truncated protein. Three-dimensional prediction models revealed that Asp69Val, Ser251Phe, and Ile115Phe caused neutral effects while Thr47Ser and Tyr79∆ produced a deleterious effect reducing VP1 stability. A549 cells infected with urine or plasma samples containing full-length VP1 variants with substitutions, sustained viral DNA replication and VP1 expression. Moreover, medium harvested from these cells was able to infect new A549 cells. In cells infected by samples with truncated VP1, MCPyV replication was hampered. In conclusion, MCPyV strains with unique mutations in the
Identifiants
pubmed: 33121182
pii: ijms21217998
doi: 10.3390/ijms21217998
pmc: PMC7663277
pii:
doi:
Substances chimiques
Capsid Proteins
0
VP1 protein, polyomavirus
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Ministero dell'Istruzione, dell'Università e della Ricerca
ID : RM11916B1DFD19A1
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