PMID- 20219911
OWN - NLM
STAT- MEDLINE
DCOM- 20100504
LR  - 20191210
IS  - 1098-5514 (Electronic)
IS  - 0022-538X (Print)
IS  - 0022-538X (Linking)
VI  - 84
IP  - 10
DP  - 2010 May
TI  - Different potential of C-type lectin-mediated entry between Marburg virus 
      strains.
PG  - 5140-7
LID - 10.1128/JVI.02021-09 [doi]
AB  - The glycoproteins (GPs) of filoviruses are responsible for virus entry into 
      cells. It is known that GP interacts with cellular C-type lectins for virus 
      attachment to cells. Since primary target cells of filoviruses express C-type 
      lectins, C-type lectin-mediated entry is thought to be a possible determinant of 
      virus tropism and pathogenesis. We compared the efficiency of C-type 
      lectin-mediated entry between Marburg virus strains Angola and Musoke by using a 
      vesicular stomatitis virus (VSV) pseudotype system. VSV pseudotyped with Angola 
      GP (VSV-Angola) infected K562 cells expressing the C-type lectin, human 
      macrophage galactose-type C-type lectin (hMGL), or dendritic cell-specific 
      ICAM-3-grabbing nonintegrin (DC-SIGN) more efficiently than VSV pseudotyped with 
      Musoke GP (VSV-Musoke). Unexpectedly, the binding affinity of the C-type lectins 
      to the carbohydrates on GPs did not correlate with the different efficiency of 
      C-type lectin-mediated entry. Site-directed mutagenesis identified the amino acid 
      at position 547, which switched the efficiency of C-type lectin-mediated entry. 
      In a three-dimensional model of GP, this amino acid was in close proximity to the 
      putative site of cathepsin processing. Interestingly, the cathepsin inhibitors 
      reduced the infectivity of VSV-Angola less efficiently than that of VSV-Musoke in 
      C-type lectin-expressing K562 cells, whereas only a limited difference was found 
      in control cells. The amino acid at position 547 was critical for the different 
      effects of the inhibitors on the virus infectivities. These results suggest that 
      the efficiency of C-type lectin-mediated entry of filoviruses is controlled not 
      only by binding affinity between C-type lectins and GP but also by mechanisms 
      underlying endosomal entry, such as proteolytic processing by the cathepsins.
FAU - Matsuno, Keita
AU  - Matsuno K
AD  - Department of Global Epidemiology, Hokkaido University Research Center for 
      Zoonosis Control, Kita-20, Nishi-10, Kita-ku, Sapporo 001-0020, Japan.
FAU - Kishida, Noriko
AU  - Kishida N
FAU - Usami, Katsuaki
AU  - Usami K
FAU - Igarashi, Manabu
AU  - Igarashi M
FAU - Yoshida, Reiko
AU  - Yoshida R
FAU - Nakayama, Eri
AU  - Nakayama E
FAU - Shimojima, Masayuki
AU  - Shimojima M
FAU - Feldmann, Heinz
AU  - Feldmann H
FAU - Irimura, Tatsuro
AU  - Irimura T
FAU - Kawaoka, Yoshihiro
AU  - Kawaoka Y
FAU - Takada, Ayato
AU  - Takada A
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20100310
PL  - United States
TA  - J Virol
JT  - Journal of virology
JID - 0113724
RN  - 0 (GP-protein, Marburg virus)
RN  - 0 (Lectins, C-Type)
RN  - 0 (Viral Envelope Proteins)
SB  - IM
MH  - Amino Acid Substitution/genetics
MH  - Animals
MH  - Cell Line
MH  - Chlorocebus aethiops
MH  - Genetic Vectors
MH  - Humans
MH  - Lectins, C-Type/*metabolism
MH  - Marburgvirus/*physiology
MH  - Models, Molecular
MH  - Mutagenesis, Site-Directed
MH  - Protein Binding
MH  - Protein Structure, Tertiary
MH  - Vesiculovirus/genetics
MH  - Viral Envelope Proteins/*metabolism
MH  - *Virus Attachment
PMC - PMC2863822
EDAT- 2010/03/12 06:00
MHDA- 2010/05/05 06:00
PMCR- 2010/11/01
CRDT- 2010/03/12 06:00
PHST- 2010/03/12 06:00 [entrez]
PHST- 2010/03/12 06:00 [pubmed]
PHST- 2010/05/05 06:00 [medline]
PHST- 2010/11/01 00:00 [pmc-release]
AID - JVI.02021-09 [pii]
AID - 2021-09 [pii]
AID - 10.1128/JVI.02021-09 [doi]
PST - ppublish
SO  - J Virol. 2010 May;84(10):5140-7. doi: 10.1128/JVI.02021-09. Epub 2010 Mar 10.