PMID- 23468635
OWN - NLM
STAT- MEDLINE
DCOM- 20130912
LR  - 20220331
IS  - 1553-7374 (Electronic)
IS  - 1553-7366 (Print)
IS  - 1553-7366 (Linking)
VI  - 9
IP  - 2
DP  - 2013 Feb
TI  - Super-resolution microscopy reveals specific recruitment of HIV-1 envelope 
      proteins to viral assembly sites dependent on the envelope C-terminal tail.
PG  - e1003198
LID - 10.1371/journal.ppat.1003198 [doi]
LID - e1003198
AB  - The inner structural Gag proteins and the envelope (Env) glycoproteins of human 
      immunodeficiency virus (HIV-1) traffic independently to the plasma membrane, 
      where they assemble the nascent virion. HIV-1 carries a relatively low number of 
      glycoproteins in its membrane, and the mechanism of Env recruitment and virus 
      incorporation is incompletely understood. We employed dual-color super-resolution 
      microscopy visualizing Gag assembly sites and HIV-1 Env proteins in 
      virus-producing and in Env expressing cells. Distinctive HIV-1 Gag assembly sites 
      were readily detected and were associated with Env clusters that always extended 
      beyond the actual Gag assembly site and often showed enrichment at the periphery 
      and surrounding the assembly site. Formation of these Env clusters depended on 
      the presence of other HIV-1 proteins and on the long cytoplasmic tail (CT) of 
      Env. CT deletion, a matrix mutation affecting Env incorporation or Env expression 
      in the absence of other HIV-1 proteins led to much smaller Env clusters, which 
      were not enriched at viral assembly sites. These results show that Env is 
      recruited to HIV-1 assembly sites in a CT-dependent manner, while Env(DeltaCT) 
      appears to be randomly incorporated. The observed Env accumulation surrounding 
      Gag assemblies, with a lower density on the actual bud, could facilitate viral 
      spread in vivo. Keeping Env molecules on the nascent virus low may be important 
      for escape from the humoral immune response, while cell-cell contacts mediated by 
      surrounding Env molecules could promote HIV-1 transmission through the 
      virological synapse.
FAU - Muranyi, Walter
AU  - Muranyi W
AD  - Department of Infectious Diseases, Virology, University Hospital Heidelberg, 
      Heidelberg, Germany.
FAU - Malkusch, Sebastian
AU  - Malkusch S
FAU - Muller, Barbara
AU  - Muller B
FAU - Heilemann, Mike
AU  - Heilemann M
FAU - Krausslich, Hans-Georg
AU  - Krausslich HG
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20130228
PL  - United States
TA  - PLoS Pathog
JT  - PLoS pathogens
JID - 101238921
RN  - 0 (HIV Envelope Protein gp120)
RN  - 0 (gag Gene Products, Human Immunodeficiency Virus)
SB  - IM
MH  - Cell Membrane/metabolism/*virology
MH  - Cluster Analysis
MH  - HIV Envelope Protein gp120/*metabolism
MH  - HeLa Cells
MH  - Humans
MH  - Microscopy, Fluorescence/*methods
MH  - Protein Conformation
MH  - Protein Structure, Tertiary
MH  - Virus Assembly/*physiology
MH  - Virus Attachment
MH  - Virus Internalization
MH  - Virus Replication
MH  - gag Gene Products, Human Immunodeficiency Virus/*metabolism
PMC - PMC3585150
COIS- The authors have declared that no competing interests exist.
EDAT- 2013/03/08 06:00
MHDA- 2013/09/13 06:00
PMCR- 2013/02/28
CRDT- 2013/03/08 06:00
PHST- 2012/08/18 00:00 [received]
PHST- 2013/01/03 00:00 [accepted]
PHST- 2013/03/08 06:00 [entrez]
PHST- 2013/03/08 06:00 [pubmed]
PHST- 2013/09/13 06:00 [medline]
PHST- 2013/02/28 00:00 [pmc-release]
AID - PPATHOGENS-D-12-02004 [pii]
AID - 10.1371/journal.ppat.1003198 [doi]
PST - ppublish
SO  - PLoS Pathog. 2013 Feb;9(2):e1003198. doi: 10.1371/journal.ppat.1003198. Epub 2013 
      Feb 28.