Unique anti-glycan antibody can lock a position of HIV tightly

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A new group of unique anti-glycan antibodies has been discovered, which tightly locks a position in HIV

Unique anti-glycan antibody can lock a position of HIV tightly.  Researchers from the Human Vaccine Institute of Duke University report that a group of newly discovered antibodies combined with the sugar coating on the HIV shell can effectively neutralize the virus and point out a new vaccine method that is also possible It is used to combat SARS-CoV-2 and fungal pathogens.

In a study published in the journal Cell, researchers described an immune cell found in monkeys and humans that produces a unique anti-glycan antibody. This new antibody has the ability to attach to a sugar plaque on the outer layer of HIV. The chain-like structure of these sugars is on the cell surface, including the outer shell of the virus. Senior author Barton Haynes, MD, director of the Human Vaccine Institute (DHVI) at Duke University, said: “This represents a new form of host defense. These new antibodies have a special shape that may be effective against various pathogens. This is very exciting.”

Haynes and colleagues Dr. Wilton Williams, director of the DHVI virus genetic analysis core, and Dr. Priyamvada Acharya, director of the DHVI Structural Biology Department, discovered this antibody in a study exploring the possibility of an immune response to sugars covering the outer surface of HIV.

More than 50% of the outer layer of the virus is composed of sugars. Haynes said that for a long time, releasing anti-carbohydrate antibodies to break down these carbohydrate structures and trigger immune B cell lymphocytes to produce antibodies to neutralize HIV is an attractive method.

“Of course, things are not that simple,” Haynes said.

Instead, HIV is coated with what looks like host sugar, forming a shield, making the virus appear to be part of the host, rather than a deadly pathogen.

But the newly discovered group of anti-glycan antibodies, called Fab-dimerized carbohydrate response (FDG) antibodies by the Duke University team, has not been discovered as a potential choice.

So far, there is only one report of a similar anti-glycan HIV antibody with an abnormal structure discovered 24 years ago (referred to as 2G12). The Duke University team has now isolated several FDG antibodies and found that they display a rare and unseen structure similar to 2G12. This structure allows the antibody to lock tightly to a specific, dense sugar spot on HIV, but not to the surface of other cells wrapped in host glycans.

Williams said: “The structural and functional characteristics of these antibodies can be used to design vaccines against this sugar on HIV, causing a B cell response that neutralizes the virus.

“These antibodies are actually much more common in blood cells than other neutralizing antibodies that target specific areas on the outer layer of HIV,” Williams said. “This is an exciting discovery because it overcomes one of the biggest complexities associated with other types of generalized neutralizing antibodies.”

Williams said that FDG antibodies can also bind to a disease-causing yeast called Candida albicans, as well as viruses, including SARS-CoV-2, which causes COVID-19. Additional research will explore how to use this antibody and deploy it on these pathogens.

(source:internet, reference only)

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