Parainfluenza hemagglutinin-neuraminidase

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Parainfluenza Hemagglutinin-Neuraminidase (HN) is a glycoprotein found on the surface of the Paramyxoviridae family of viruses, which includes the parainfluenza virus. This glycoprotein plays a crucial role in the virus's ability to infect host cells. It combines both hemagglutinin and neuraminidase activities, which are essential for the virus's life cycle, including attachment to host cells, entry, and release of progeny viruses.

Function[edit | edit source]

The HN glycoprotein has dual functions due to its combined activities. The hemagglutinin activity allows the virus to bind to sialic acid residues on the surface of host cells, facilitating viral entry. The neuraminidase activity, on the other hand, helps in the release of newly formed virus particles from the host cell by cleaving sialic acid residues, preventing the aggregation of viruses and promoting their spread to infect new cells.

Structure[edit | edit source]

The HN glycoprotein is a type II membrane protein that forms tetramers on the surface of the virus. Its structure is crucial for its function, with specific domains responsible for its hemaglutinin and neuraminidase activities. Understanding the structure of HN is important for the development of antiviral drugs and vaccines targeting the parainfluenza virus.

Clinical Significance[edit | edit source]

Infections caused by the parainfluenza virus can range from mild respiratory illnesses to severe conditions such as pneumonia, particularly in children, the elderly, and immunocompromised individuals. The HN glycoprotein is a target for vaccine development due to its critical role in the virus's infectivity and its immune-dominant nature. Inhibitors targeting the neuraminidase activity of HN have also been explored as potential antiviral therapies.

Research and Development[edit | edit source]

Research into the HN glycoprotein includes studies on its structure-function relationships, mechanisms of action, and its role in the immune response to parainfluenza virus infection. Advances in this area could lead to the development of more effective vaccines and antiviral drugs against the parainfluenza virus and other members of the Paramyxoviridae family.

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Contributors: Prab R. Tumpati, MD