PMID- 8797709
OWN - NLM
STAT- MEDLINE
DCOM- 19961029
LR  - 20191024
IS  - 1077-9450 (Print)
IS  - 1077-9450 (Linking)
VI  - 13 Suppl 1
DP  - 1996
TI  - The HTLV-I envelope glycoproteins: structure and functions.
PG  - S85-91
AB  - The human T-cell lymphotropic virus type I (HTLV-I) envelope has a structural 
      organization shared by all retroviral envelopes, which contain two mature viral 
      glycoproteins deriving from a common precursor: an external surface protein (SU), 
      associated with a transmembrane protein (TM) responsible for anchoring the SU-TM 
      complex at the cell surface or in the viral envelope. Our understanding of the 
      tertiary structure of these proteins is extremely poor. The intracellular 
      maturation follows the normal cellular secretory pathway, resulting in expression 
      of the mature glycoproteins at the cell surface. The five potential 
      N-glycosylation sites are glycosylated. Most mutations artificially introduced 
      into the glycoproteins result in loss of function, mostly due to abnormal 
      intracellular maturation. This probably indicates a very compact structure of 
      these proteins, where the entire structure is involved in correct conformation. 
      Studies using neutralizing antibodies or mutagenesis have defined functional 
      domains in the SU protein, which is responsible for receptor binding. These 
      domains occur throughout the SU glycoprotein. Sequence analysis of the HTLV-I TM 
      predicts a structure, and probably functions, similar to other retrovirus TMs: 
      involvement of this glycoprotein in the different oligomerization steps leading 
      to a fusogenic SU-TM complex and in the fusion process itself. These features 
      remain to be proven, and it is not yet understood why the free HTLV-I viral 
      particle is not infectious.
FAU - Delamarre, L
AU  - Delamarre L
AD  - CNRS URA 1156, Institut Gustave Roussy, Villejuif, France.
FAU - Rosenberg, A R
AU  - Rosenberg AR
FAU - Pique, C
AU  - Pique C
FAU - Pham, D
AU  - Pham D
FAU - Callebaut, I
AU  - Callebaut I
FAU - Dokhelar, M C
AU  - Dokhelar MC
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
PL  - United States
TA  - J Acquir Immune Defic Syndr Hum Retrovirol
JT  - Journal of acquired immune deficiency syndromes and human retrovirology : 
      official publication of the International Retrovirology Association
JID - 9501482
RN  - 0 (Glycoproteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (Receptors, Cell Surface)
RN  - 0 (Viral Envelope Proteins)
SB  - IM
MH  - Amino Acid Sequence
MH  - Genetic Variation
MH  - Glycoproteins/*chemistry/genetics/*physiology
MH  - Human T-lymphotropic virus 1/*chemistry/genetics/*physiology
MH  - Membrane Proteins/metabolism/physiology
MH  - Molecular Sequence Data
MH  - Receptors, Cell Surface/physiology
MH  - T-Lymphocytes/virology
MH  - Viral Envelope Proteins/*chemistry/genetics/*physiology
MH  - *Virus Assembly
RF  - 54
EDAT- 1996/01/01 00:00
MHDA- 1996/01/01 00:01
CRDT- 1996/01/01 00:00
PHST- 1996/01/01 00:00 [pubmed]
PHST- 1996/01/01 00:01 [medline]
PHST- 1996/01/01 00:00 [entrez]
AID - 10.1097/00042560-199600001-00015 [doi]
PST - ppublish
SO  - J Acquir Immune Defic Syndr Hum Retrovirol. 1996;13 Suppl 1:S85-91. doi: 
      10.1097/00042560-199600001-00015.