C-type lectins do not act as functional receptors for filovirus entry into cells

Keita Matsuno, Eri Nakayama, Osamu Noyori, Andrea Marzi, Hideki Ebihara, Tatsuro Irimura, Heinz Feldmann, Ayato Takada

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

Cellular C-type lectins have been reported to facilitate filovirus infection by binding to glycans on filovirus glycoprotein (GP). However, it is not clearly known whether interaction between C-type lectins and GP mediates all the steps of virus entry (i.e., attachment, internalization, and membrane fusion). In this study, we generated vesicular stomatitis viruses pseudotyped with mutant GPs that have impaired structures of the putative receptor binding regions and thus reduced ability to infect the monkey kidney cells that are routinely used for virus propagation. We found that infectivities of viruses with the mutant GPs dropped in C-type lectin-expressing cells, parallel with those in the monkey kidney cells, whereas binding activities of these GPs to the C-type lectins were not correlated with the reduced infectivities. These results suggest that C-type lectin-mediated entry of filoviruses requires other cellular molecule(s) that may be involved in virion internalization or membrane fusion.

Original languageEnglish (US)
Pages (from-to)144-148
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume403
Issue number1
DOIs
StatePublished - Dec 3 2010
Externally publishedYes

Fingerprint

C-Type Lectins
Viruses
Membrane Fusion
Haplorhini
Glycoproteins
Fusion reactions
Membranes
Kidney
Virus Internalization
Vesicular Stomatitis
Virion
Polysaccharides
Molecules
Infection

Keywords

  • C-type lectin
  • Filovirus
  • Virus entry

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Molecular Biology

Cite this

C-type lectins do not act as functional receptors for filovirus entry into cells. / Matsuno, Keita; Nakayama, Eri; Noyori, Osamu; Marzi, Andrea; Ebihara, Hideki; Irimura, Tatsuro; Feldmann, Heinz; Takada, Ayato.

In: Biochemical and Biophysical Research Communications, Vol. 403, No. 1, 03.12.2010, p. 144-148.

Research output: Contribution to journalArticle

Matsuno, K, Nakayama, E, Noyori, O, Marzi, A, Ebihara, H, Irimura, T, Feldmann, H & Takada, A 2010, 'C-type lectins do not act as functional receptors for filovirus entry into cells', Biochemical and Biophysical Research Communications, vol. 403, no. 1, pp. 144-148. https://doi.org/10.1016/j.bbrc.2010.10.136
Matsuno, Keita ; Nakayama, Eri ; Noyori, Osamu ; Marzi, Andrea ; Ebihara, Hideki ; Irimura, Tatsuro ; Feldmann, Heinz ; Takada, Ayato. / C-type lectins do not act as functional receptors for filovirus entry into cells. In: Biochemical and Biophysical Research Communications. 2010 ; Vol. 403, No. 1. pp. 144-148.
@article{cdf53ef7ba624d7588c170732fd1ef3e,
title = "C-type lectins do not act as functional receptors for filovirus entry into cells",
abstract = "Cellular C-type lectins have been reported to facilitate filovirus infection by binding to glycans on filovirus glycoprotein (GP). However, it is not clearly known whether interaction between C-type lectins and GP mediates all the steps of virus entry (i.e., attachment, internalization, and membrane fusion). In this study, we generated vesicular stomatitis viruses pseudotyped with mutant GPs that have impaired structures of the putative receptor binding regions and thus reduced ability to infect the monkey kidney cells that are routinely used for virus propagation. We found that infectivities of viruses with the mutant GPs dropped in C-type lectin-expressing cells, parallel with those in the monkey kidney cells, whereas binding activities of these GPs to the C-type lectins were not correlated with the reduced infectivities. These results suggest that C-type lectin-mediated entry of filoviruses requires other cellular molecule(s) that may be involved in virion internalization or membrane fusion.",
keywords = "C-type lectin, Filovirus, Virus entry",
author = "Keita Matsuno and Eri Nakayama and Osamu Noyori and Andrea Marzi and Hideki Ebihara and Tatsuro Irimura and Heinz Feldmann and Ayato Takada",
year = "2010",
month = "12",
day = "3",
doi = "10.1016/j.bbrc.2010.10.136",
language = "English (US)",
volume = "403",
pages = "144--148",
journal = "Biochemical and Biophysical Research Communications",
issn = "0006-291X",
publisher = "Academic Press Inc.",
number = "1",

}

TY - JOUR

T1 - C-type lectins do not act as functional receptors for filovirus entry into cells

AU - Matsuno, Keita

AU - Nakayama, Eri

AU - Noyori, Osamu

AU - Marzi, Andrea

AU - Ebihara, Hideki

AU - Irimura, Tatsuro

AU - Feldmann, Heinz

AU - Takada, Ayato

PY - 2010/12/3

Y1 - 2010/12/3

N2 - Cellular C-type lectins have been reported to facilitate filovirus infection by binding to glycans on filovirus glycoprotein (GP). However, it is not clearly known whether interaction between C-type lectins and GP mediates all the steps of virus entry (i.e., attachment, internalization, and membrane fusion). In this study, we generated vesicular stomatitis viruses pseudotyped with mutant GPs that have impaired structures of the putative receptor binding regions and thus reduced ability to infect the monkey kidney cells that are routinely used for virus propagation. We found that infectivities of viruses with the mutant GPs dropped in C-type lectin-expressing cells, parallel with those in the monkey kidney cells, whereas binding activities of these GPs to the C-type lectins were not correlated with the reduced infectivities. These results suggest that C-type lectin-mediated entry of filoviruses requires other cellular molecule(s) that may be involved in virion internalization or membrane fusion.

AB - Cellular C-type lectins have been reported to facilitate filovirus infection by binding to glycans on filovirus glycoprotein (GP). However, it is not clearly known whether interaction between C-type lectins and GP mediates all the steps of virus entry (i.e., attachment, internalization, and membrane fusion). In this study, we generated vesicular stomatitis viruses pseudotyped with mutant GPs that have impaired structures of the putative receptor binding regions and thus reduced ability to infect the monkey kidney cells that are routinely used for virus propagation. We found that infectivities of viruses with the mutant GPs dropped in C-type lectin-expressing cells, parallel with those in the monkey kidney cells, whereas binding activities of these GPs to the C-type lectins were not correlated with the reduced infectivities. These results suggest that C-type lectin-mediated entry of filoviruses requires other cellular molecule(s) that may be involved in virion internalization or membrane fusion.

KW - C-type lectin

KW - Filovirus

KW - Virus entry

UR - http://www.scopus.com/inward/record.url?scp=78649710743&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=78649710743&partnerID=8YFLogxK

U2 - 10.1016/j.bbrc.2010.10.136

DO - 10.1016/j.bbrc.2010.10.136

M3 - Article

C2 - 21056544

AN - SCOPUS:78649710743

VL - 403

SP - 144

EP - 148

JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

SN - 0006-291X

IS - 1

ER -