HIV is different in structure from other
retroviruses. It is roughly spherical with a diameter of about 120nm, around 60
times smaller than a red-blood cell, yet large for a virus. It is composed of
two copies of positive single-stranded RNA that codes for the virus’s nine genes
enclose by a conical capsid composed of 2,000 copies of the viral protein p24.
retroviruses. It is roughly spherical with a diameter of about 120nm, around 60
times smaller than a red-blood cell, yet large for a virus. It is composed of
two copies of positive single-stranded RNA that codes for the virus’s nine genes
enclose by a conical capsid composed of 2,000 copies of the viral protein p24.
The single stranded RNA is tightly bound to
nucleo-capsid protein p7 and enzymes needed for the development of the virus
such as reverse transcriptase, protase, ribonuclease and integrase. A matrix
composed of the viral protein p17 surrounds the capsid ensuring the integrity
of the viron particle.
nucleo-capsid protein p7 and enzymes needed for the development of the virus
such as reverse transcriptase, protase, ribonuclease and integrase. A matrix
composed of the viral protein p17 surrounds the capsid ensuring the integrity
of the viron particle.
This is in turn surrounded by an envelope of host
cell origin. The envelope is formed when the capsid buds from the host cell,
taking some of the host cell membrane with it. The envelopes include the
glycoprotein gp120 and gp41. As a result of it role in virus cell attachment,
the structure of the virus envelop spike, consisting of gp120 and gp41 is of
particular importance (Scarlata and Carter, 2003).
cell origin. The envelope is formed when the capsid buds from the host cell,
taking some of the host cell membrane with it. The envelopes include the
glycoprotein gp120 and gp41. As a result of it role in virus cell attachment,
the structure of the virus envelop spike, consisting of gp120 and gp41 is of
particular importance (Scarlata and Carter, 2003).
Reference
Scarlata, C. and Carter, C (2003): Role of
Myristoylation in HIV-1 Gag Assembly, Biochemistry,
42:6408-6417.
Myristoylation in HIV-1 Gag Assembly, Biochemistry,
42:6408-6417.
