Since the discovery of HIV (human immunodeficiency virus) in 1983, the genome and protein structure of this virus have been the focus of scientific research. Initially, it was thought to be related to human T-cell leukemia virus (HTLV), but during research at the Pasteur Institute in France, scientists isolated this new genetically different retrovirus from AIDS patients and later identified it as It's named HIV.
Each HIV virion consists of a viral envelope and related matrix structures, surrounded by a shell, which contains two single-stranded RNA genomes and several enzymes.
HIV is structurally different from other retroviruses. The HIV virus particle is about 100 nanometers in diameter, and its internal region includes a concave core that contains not only two copies (+ strand) of the single-stranded RNA genome, but also important enzymes such as reverse transcriptase, integrase, and protease. HIV's RNA genome is encoded by eight viral proteins that are critical to the HIV life cycle.
The HIV genome contains 9 genes, which encode 15 viral proteins and are synthesized in the form of polypeptides. These polypeptides can produce structural proteins within the virus, viral enzymes or glycoproteins of the viral envelope.
HIV utilizes a complex differential RNA splicing system to obtain nine different gene products from a genome of less than 10 kb.
The functions of these genes include the production of structural proteins as well as regulating and assisting protein synthesis. In particular, the gag gene provides the basic physical structure of the virus, while the pol gene is the basis of the retrovirus regeneration mechanism.
Some key proteins of HIV include:
gag
gene: encodes the precursor gag polypeptide, which is processed into structural proteins by viral protease during virus maturation. pol
gene: Responsible for encoding reverse transcriptase and integrase. These enzymes are key in the virus life cycle. env
gene: encodes an envelope glycoprotein, which is mainly responsible for binding to the CD4 receptor of the host cell and promoting the virus to enter the cell. Among them, gp120 and gp41 encoded by env
are the most important glycoproteins in the HIV infection process and are the main targets for vaccine development.
The structure of the Env protein is very special, with a high concentration of N-chain glycosylation, which can effectively block the neutralization of HIV by antibodies.
This highly glycosylated structure makes HIV an extremely challenging pathogen, and scientists have been working hard to find a vaccine that can overcome this protection.
HIV also has a variety of regulatory proteins, such as tat and rev, etc. These proteins play an important role in HIV gene expression and viral replication. The presence of these proteins can regulate the life cycle of HIV in host cells. Auxiliary proteins such as Vpr, Vif, and Nef affect the infectivity of the virus and the response of the host cell.
The RNA structure of HIV not only includes the terminal 5' untranslated region (UTR), but also contains some conserved secondary structures, which can regulate the process of viral reverse transcription. Including the transcription activation region (TAR), viral packaging structure, etc., these secondary structures are considered to have an important impact on the life cycle of HIV.
The V3 loop is part of the HIV virus coat glycoprotein gp120, which enables the virus to successfully infect human immune cells. This structure not only provides the possibility for the virus to enter host cells, but also becomes a key target for treatment and vaccine development.
With the deepening of research, scientists have gradually solved the mystery of HIV's structure and function. Although significant progress has been made, there are still many problems to be solved. For example, what kind of breakthroughs can such a cleverly designed virus bring about in future vaccine development?