HSS 2305 A - Lecture 14 Quiz

The genetic material of HIV is single-stranded RNA (ssRNA) but can also be double-stranded RNA (dsRNA) in some cases. This RNA contains the instructions for building new HIV particles.

HIV invades the central nervous system, leading to severe neurological disorders. This can result in cognitive decline, movement problems, and other neurological issues.

HIV weakens the immune system, making the body more susceptible to infections and diseases. This suppression of the immune system is a major consequence of HIV infection.

Three essential genes - gag, pol, and env - present in all retroviruses, provide instructions for building structural proteins needed for new virus particles.

An enzyme encoded by the 'pol' gene, HIV protease cleaves the gag/pol polyproteins, generating essential viral enzymes and structural proteins required for virus replication.

Six additional genes: tat, rev, nef, vif, vpr, and vpu (or vpx for HIV-2), regulate proteins that control HIV's ability to infect cells, replicate, and cause disease.

HIV primarily infects T4 lymphocytes, which are critical for immune function. These cells have CD4 receptors that HIV uses to enter and replicate within them.

A key enzyme in HIV's life cycle, reverse transcriptase catalyzes the synthesis of DNA from the viral RNA template. This DNA is then integrated into the host cell genome, allowing HIV to replicate silently within the cells.

A precursor protein of the HIV envelope glycoprotein, which undergoes cleavage to form gp120 and gp41.

The external glycoprotein of the HIV envelope, responsible for binding to the CD4 receptor on host cells.

The transmembrane glycoprotein of the HIV envelope, responsible for mediating fusion of the viral envelope with the host cell membrane.

Helical domains within gp41 that interact and form a complex, crucial for the fusion process with the host cell membrane.

A complex structure formed by the interaction of HR-N and HR-C domains, driving fusion with the host membrane.

A specific amino acid sequence commonly found in proteins, consisting of 7 repeating units. The sequence alternates between hydrophobic (Hd), polar (Po), and charged (Ch) amino acids.

Protein molecules that stick out from the surface of the HIV virus. These molecules are shaped like mushrooms, with a stem (gp41) and a cap (gp120).

A medication used to treat HIV infection. It acts by blocking the reverse transcriptase enzyme, preventing the virus from replicating.

An enzyme found in HIV that inserts the viral DNA into the host cell's DNA, allowing the virus to replicate.

An enzyme found in HIV that cuts up viral proteins to build new viral particles. This is another critical step in the virus's replication cycle.

A therapy that prevents HIV from attaching to healthy cells. This is done using antibodies that bind to the virus's gp41 or gp120 proteins, or by using soluble CD4 (a protein that mimics the cell's CD4 receptor to block the virus's entry).

A specific type of antibody that targets a single protein. In the context of HIV, monoclonal antibodies can be used to target the cell's CD4 protein, blocking HIV's attachment and infection.

The influenza virus is a spherical structure containing negative-stranded RNA. Its outer membrane contains two key proteins: Hemagglutinin (HA) and Neuraminidase (NA), both anchored to the inner lipid bilayer by M-proteins.

This glycoprotein is responsible for attaching the influenza virus to host cells by binding to sialic acid receptors on the surface of cells.

This glycoprotein helps the influenza virus escape from infected cells by cleaving the sialic acid receptors.

Influenza viruses are classified based on the type of Hemagglutinin (H) and Neuraminidase (N) proteins they possess. Different combinations of these proteins create various subtypes.

The H5N1 strain of avian influenza virus is highly infectious and pathogenic, causing high mortality rates in birds, especially chickens. Although it normally doesn't replicate in humans, it has the potential to cause severe disease.

hSARS CoV, or Human Severe Acute Respiratory Syndrome Coronavirus, is a type of coronavirus that causes severe respiratory illness, including pneumonia. It was first reported in 2002, and it can be highly infectious, spreading quickly across countries.

While other coronaviruses like hCoV-229E and hCoV-OC43 cause common colds, hSARS CoV is different because it can cause severe pneumonia and respiratory distress. It's a new type of coronavirus.

hSARS CoV is highly contagious and can spread quickly from person to person through respiratory droplets, such as when an infected person coughs or sneezes.

Individuals infected with hSARS CoV experience symptoms like fever, cough, shortness of breath, and difficulty breathing. In severe cases, it can lead to respiratory failure.

HIV Protease Inhibitors (PIs) are drugs used to treat HIV by blocking the activity of a viral enzyme called protease. By blocking protease, PIs help prevent the HIV virus from replicating.

While effective, PIs can cause side effects like increased blood sugar, leading to diabetes in some HIV patients. They can also raise blood sugar levels (hyperglycemia) in those already using them.

Alternate Combination Therapy involves using a combination of three different HIV drugs: Nucleoside Reverse Transcriptase Inhibitors (NRTIs), Non-Nucleoside Reverse Transcriptase Inhibitors (NNRTIs) and Protease Inhibitors (PIs). This helps combat drug resistance and improve treatment effectiveness.

HIV is known for its ability to develop resistance to antiretroviral drugs. This means that the virus can adapt and become less sensitive to the medication over time, making treatment less effective.

HIV protease, an enzyme essential for viral replication, only functions in its dimeric form, meaning it needs two identical protein units to work. This dimeric form enables the enzyme to bind and cleave viral proteins, allowing the virus to mature and replicate.

The active site of HIV protease is where the enzyme binds to and cleaves viral proteins. Within the active site, the "Asp-Thr-Gly (D-T-G)" sequence plays a crucial role, acting like a scissors that cut the proteins apart.

A flexible 'flap' region within HIV protease, located in the amino acid sequence [residue 43-58], interacts with the substrate, aiding in the cleavage process. It helps position the protein for cleavage by the active site.

Drugs that specifically block HIV protease, preventing the enzyme from cleaving viral proteins. By inhibiting the protease, the virus cannot mature and replicate effectively.

Inhibiting the activity of host cell proteases like Furin/PCSK3, which is responsible for cleaving gp160 into gp120 and gp41, can block HIV infection. This stops the formation of the viral envelope complex needed for attachment to host cells.

The precursor protein gp160, found on the surface of HIV, undergoes cleavage by host proteases like Furin, producing gp120 and gp41. This process is critical for the formation of the viral envelope and subsequent attachment to host cells.

Targeting multiple points in the HIV life cycle simultaneously, using a combination of drugs, can effectively suppress viral pathogenesis. This approach combines targeting host proteases like Furin, viral proteases like HIV protease, and the viral fusion process to block HIV's ability to infect and spread.

Targeting Furin, a host protease essential for gp160 processing, with specific inhibitors can block the formation of the viral envelope and prevent the virus from attaching to and entering host cells. This approach is potentially very effective in suppressing HIV infection.