PMID- 17950396
OWN - NLM
STAT- MEDLINE
DCOM- 20080910
LR  - 20211109
IS  - 0042-6822 (Print)
IS  - 0042-6822 (Linking)
VI  - 371
IP  - 1
DP  - 2008 Feb 5
TI  - Adenovirus dodecahedron cell attachment and entry are mediated by heparan sulfate 
      and integrins and vary along the cell cycle.
PG  - 155-64
AB  - The adenovirus penton base is a strategic protein involved in the virus 
      internalisation pathway through interaction between its RGD sequences and 
      integrin. In some human adenovirus serotypes, this pentameric protein features 
      the ability of interacting together by twelve, leading to the formation of a 
      symmetric nanoparticle called dodecahedron (Dd). This non-infectious 
      adenovirus-like particle exhibiting sixty RGD sequences interacts with integrin 
      but also with heparan sulfate proteoglycans (HSPGs) expressed at the cell 
      surface. In this study, we discriminate the respective importance of HSPGs and 
      integrin on human adenovirus serotype 3 dodecahedron attachment and entry. Using 
      different cell lines and a specific integrin inhibitor, we have determined that 
      HSPGs are mainly responsible for particle attachment to the cell surface, 
      favouring a strictly required interaction with integrin that triggers 
      internalisation. No other receptors are involved in Dd entry and integrins on 
      their own can mediate the particle entry in HSPGs-deficient cells. Moreover, 
      integrin recognition by Dd is highly susceptible to cations and particularly to 
      manganese that enhances particle binding by 4- to 7-fold compared to calcium. 
      Interestingly, investigations on Dd receptors along the cell cycle revealed an 
      enhanced particle targeting to mitotic cells and a loss of internalisation at 
      this stage. This phenomenon observed with both HeLa- and HSPGs-deficient cells, 
      depends on integrin remodelling during mitosis. This provides new clues for the 
      use of this adenovirus nanoparticle as a delivery vector and sheds light on the 
      integrin and HSPGs relationship in both resting and dividing cells.
FAU - Fender, Pascal
AU  - Fender P
AD  - CNRS, CEA, UJF: Institut de Biologie Structurale, 41 rue Jules Horowitz 38027 
      Grenoble, France. pascal.fender@ibs.fr
FAU - Schoehn, Guy
AU  - Schoehn G
FAU - Perron-Sierra, Francoise
AU  - Perron-Sierra F
FAU - Tucker, Gordon C
AU  - Tucker GC
FAU - Lortat-Jacob, Hugues
AU  - Lortat-Jacob H
LA  - eng
PT  - Journal Article
DEP - 20071022
PL  - United States
TA  - Virology
JT  - Virology
JID - 0110674
RN  - 0 (Capsid Proteins)
RN  - 0 (Integrins)
RN  - 0 (Proteoglycans)
RN  - 0 (heparin proteoglycan)
RN  - 9005-49-6 (Heparin)
SB  - IM
MH  - Adenoviruses, Human/*physiology/ultrastructure
MH  - Animals
MH  - CHO Cells
MH  - Capsid Proteins/*metabolism
MH  - Cell Adhesion/physiology
MH  - *Cell Cycle
MH  - Cricetinae
MH  - Cricetulus
MH  - HeLa Cells
MH  - Heparin/*analogs & derivatives/physiology
MH  - Humans
MH  - Integrins/*physiology
MH  - Proteoglycans/*physiology
EDAT- 2007/10/24 09:00
MHDA- 2008/09/11 09:00
CRDT- 2007/10/24 09:00
PHST- 2007/07/05 00:00 [received]
PHST- 2007/08/22 00:00 [revised]
PHST- 2007/09/07 00:00 [accepted]
PHST- 2007/10/24 09:00 [pubmed]
PHST- 2008/09/11 09:00 [medline]
PHST- 2007/10/24 09:00 [entrez]
AID - S0042-6822(07)00594-6 [pii]
AID - 10.1016/j.virol.2007.09.026 [doi]
PST - ppublish
SO  - Virology. 2008 Feb 5;371(1):155-64. doi: 10.1016/j.virol.2007.09.026. Epub 2007 
      Oct 22.