Academic Journal
Προβολή σε EDS

Host glycocalyx captures HIV proximal to the cell surface via oligomannose-GlcNAc glycan-glycan interactions to support viral entry

Λεπτομέρειες βιβλιογραφικής εγγραφής
Τίτλος: Host glycocalyx captures HIV proximal to the cell surface via oligomannose-GlcNAc glycan-glycan interactions to support viral entry
Συγγραφείς: Spillings, BL, Day, CJ, Garcia-Minambres, A, Aggarwal, A, Condon, ND, Haselhorst, T, Purcell, DFJ, Turville, SG, Stow, JL, Jennings, MP, Mak, J
Στοιχεία εκδότη: CELL PRESS
Έτος έκδοσης: 2022
Συλλογή: The University of Melbourne: Digital Repository
Περιγραφή: Here, we present ultrastructural analyses showing that incoming HIV are captured near the lymphocyte surface in a virion-glycan-dependent manner. Biophysical analyses show that removal of either virion- or cell-associated N-glycans impairs virus-cell binding, and a similar glycan-dependent relationship is observed between purified HIV envelope (Env) and primary T cells. Trimming of N-glycans from either HIV or Env does not inhibit protein-protein interactions. Glycan arrays reveal HIV preferentially binds to N-acetylglucosamine and mannose. Interfering with these glycan-based interactions reduces HIV infectivity. These glycan interactions are distinct from previously reported glycan-lectin and non-specific electrostatic charge-based interactions. Specific glycan-glycan-mediated attachment occurs prior to virus entry and enhances efficiency of infection. Binding and fluorescent imaging data support glycan-glycan interactions as being responsible, at least in part, for initiating contact between HIV and the host cell, prior to viral Env-cellular CD4 engagement.
Τύπος εγγράφου: article in journal/newspaper
Γλώσσα: English
ISSN: 2211-1247
Relation: https://hdl.handle.net/11343/302532
Διαθεσιμότητα: https://hdl.handle.net/11343/302532
Rights: https://creativecommons.org/licenses/by-nc-nd/4.0 ; CC BY-NC-ND
Αριθμός Καταχώρησης: edsbas.CCDDEC63
Βάση Δεδομένων: BASE
FullText Text:
  Availability: 0
CustomLinks:
  – Url: https://hdl.handle.net/11343/302532#
    Name: EDS - BASE (ns324271)
    Category: fullText
    Text: View record from BASE
  – Url: https://www.sciencedirect.com/science/link?ref_val_fmt=info:ofi/fmt:kev:mtx:journal&svc_val_fmt=info:ofi/fmt:kev:mtx:sch_srv&rfr_dat=saltver:1&rfr_dat=origin:EBSCOLINK&ctx_enc=info:ofi/enc:UTF-8&ctx_ver=Z39.88-2004&svc.fulltext=yes&rft.issn=22111247&rft.volume=&rft.title=Host glycocalyx captures HIV proximal to the cell surface via oligomannose-GlcNAc glycan-glycan interactions to support viral entry
    Name: ScienceDirect (all content) (s7799221)
    Category: fullText
    Text: View record from ScienceDirect
    MouseOverText: View record from ScienceDirect
  – Url: https://resolver.ebsco.com/c/fiv2js/result?sid=EBSCO:edsbas&genre=article&issn=22111247&ISBN=&volume=&issue=&date=20220101&spage=&pages=&title=Host glycocalyx captures HIV proximal to the cell surface via oligomannose-GlcNAc glycan-glycan interactions to support viral entry&atitle=Host%20glycocalyx%20captures%20HIV%20proximal%20to%20the%20cell%20surface%20via%20oligomannose-GlcNAc%20glycan-glycan%20interactions%20to%20support%20viral%20entry&aulast=Spillings%2C%20BL&id=DOI:
    Name: Full Text Finder (for New FTF UI) (ns324271)
    Category: fullText
    Text: Full Text Finder
    MouseOverText: Full Text Finder
Header DbId: edsbas
DbLabel: BASE
An: edsbas.CCDDEC63
RelevancyScore: 920
AccessLevel: 3
PubType: Academic Journal
PubTypeId: academicJournal
PreciseRelevancyScore: 920.2763671875
IllustrationInfo
Items – Name: Title
  Label: Title
  Group: Ti
  Data: Host glycocalyx captures HIV proximal to the cell surface via oligomannose-GlcNAc glycan-glycan interactions to support viral entry
– Name: Author
  Label: Authors
  Group: Au
  Data: <searchLink fieldCode="AR" term="%22Spillings%2C+BL%22">Spillings, BL</searchLink><br /><searchLink fieldCode="AR" term="%22Day%2C+CJ%22">Day, CJ</searchLink><br /><searchLink fieldCode="AR" term="%22Garcia-Minambres%2C+A%22">Garcia-Minambres, A</searchLink><br /><searchLink fieldCode="AR" term="%22Aggarwal%2C+A%22">Aggarwal, A</searchLink><br /><searchLink fieldCode="AR" term="%22Condon%2C+ND%22">Condon, ND</searchLink><br /><searchLink fieldCode="AR" term="%22Haselhorst%2C+T%22">Haselhorst, T</searchLink><br /><searchLink fieldCode="AR" term="%22Purcell%2C+DFJ%22">Purcell, DFJ</searchLink><br /><searchLink fieldCode="AR" term="%22Turville%2C+SG%22">Turville, SG</searchLink><br /><searchLink fieldCode="AR" term="%22Stow%2C+JL%22">Stow, JL</searchLink><br /><searchLink fieldCode="AR" term="%22Jennings%2C+MP%22">Jennings, MP</searchLink><br /><searchLink fieldCode="AR" term="%22Mak%2C+J%22">Mak, J</searchLink>
– Name: Publisher
  Label: Publisher Information
  Group: PubInfo
  Data: CELL PRESS
– Name: DatePubCY
  Label: Publication Year
  Group: Date
  Data: 2022
– Name: Subset
  Label: Collection
  Group: HoldingsInfo
  Data: The University of Melbourne: Digital Repository
– Name: Abstract
  Label: Description
  Group: Ab
  Data: Here, we present ultrastructural analyses showing that incoming HIV are captured near the lymphocyte surface in a virion-glycan-dependent manner. Biophysical analyses show that removal of either virion- or cell-associated N-glycans impairs virus-cell binding, and a similar glycan-dependent relationship is observed between purified HIV envelope (Env) and primary T cells. Trimming of N-glycans from either HIV or Env does not inhibit protein-protein interactions. Glycan arrays reveal HIV preferentially binds to N-acetylglucosamine and mannose. Interfering with these glycan-based interactions reduces HIV infectivity. These glycan interactions are distinct from previously reported glycan-lectin and non-specific electrostatic charge-based interactions. Specific glycan-glycan-mediated attachment occurs prior to virus entry and enhances efficiency of infection. Binding and fluorescent imaging data support glycan-glycan interactions as being responsible, at least in part, for initiating contact between HIV and the host cell, prior to viral Env-cellular CD4 engagement.
– Name: TypeDocument
  Label: Document Type
  Group: TypDoc
  Data: article in journal/newspaper
– Name: Language
  Label: Language
  Group: Lang
  Data: English
– Name: ISSN
  Label: ISSN
  Group: ISSN
  Data: 2211-1247
– Name: NoteTitleSource
  Label: Relation
  Group: SrcInfo
  Data: https://hdl.handle.net/11343/302532
– Name: URL
  Label: Availability
  Group: URL
  Data: https://hdl.handle.net/11343/302532
– Name: Copyright
  Label: Rights
  Group: Cpyrght
  Data: https://creativecommons.org/licenses/by-nc-nd/4.0 ; CC BY-NC-ND
– Name: AN
  Label: Accession Number
  Group: ID
  Data: edsbas.CCDDEC63
PLink https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=edsbas&AN=edsbas.CCDDEC63
RecordInfo BibRecord:
  BibEntity:
    Languages:
      – Text: English
    Titles:
      – TitleFull: Host glycocalyx captures HIV proximal to the cell surface via oligomannose-GlcNAc glycan-glycan interactions to support viral entry
        Type: main
  BibRelationships:
    HasContributorRelationships:
      – PersonEntity:
          Name:
            NameFull: Spillings, BL
      – PersonEntity:
          Name:
            NameFull: Day, CJ
      – PersonEntity:
          Name:
            NameFull: Garcia-Minambres, A
      – PersonEntity:
          Name:
            NameFull: Aggarwal, A
      – PersonEntity:
          Name:
            NameFull: Condon, ND
      – PersonEntity:
          Name:
            NameFull: Haselhorst, T
      – PersonEntity:
          Name:
            NameFull: Purcell, DFJ
      – PersonEntity:
          Name:
            NameFull: Turville, SG
      – PersonEntity:
          Name:
            NameFull: Stow, JL
      – PersonEntity:
          Name:
            NameFull: Jennings, MP
      – PersonEntity:
          Name:
            NameFull: Mak, J
    IsPartOfRelationships:
      – BibEntity:
          Dates:
            – D: 01
              M: 01
              Type: published
              Y: 2022
          Identifiers:
            – Type: issn-print
              Value: 22111247
            – Type: issn-locals
              Value: edsbas
            – Type: issn-locals
              Value: edsbas.oa
ResultId 1