Researchers found that an antibody, 2B7, blocks the effects of dengue virus infection and other similar diseases in a joint study published Jan. 8 from UC Berkeley and the University of Michigan.

The study found that 2B7 prevents the ability of the dengue virus to cause disease in mice, according to a University of Michigan press release. Researchers were able to find the regions of nonstructural protein 1, or NS1, that the antibody binds to, which could be used in future research to develop therapeutics, according to UC Berkeley postdoctoral scholar Scott Biering.

“This paper is significant as it provides the first structural and mechanistic characterisation of a broad-spectrum NS1 antibody-mediated protection against current and emerging flaviviruses,” said campus graduate researcher and doctoral candidate Nicholas Lo in an email.

In theory, Biering added, researchers could identify treatments for flaviviruses such as dengue virus, Zika virus, West Nile virus, Japanese encephalitis and yellow fever, among others.

According to Biering, one of the struggles with flaviviruses is that while they have similar basic biology, their proteins are different enough such that antibodies against one do not necessarily bind strongly to the proteins of another. In practice, this means that someone who is bitten by a mosquito with one type of dengue may get sick and then gain antibodies against that type, but not against other types of dengue, and symptoms from other flaviviruses may actually worsen.

“You can either redesign your vaccine so it’s so good that it neutralizes against all four serotypes, which is tough and kind of trying to hit a moving target, or you can target proteins that are also important for causing disease,” Biering said.

Traditional vaccine development efforts against dengue and other flaviviruses focus on the envelope protein, or E, on the virus surface, but the breadth of protection from these vaccines is limited, according to Lo.

This research alternatively targets NS1 as a potential therapeutic and vaccine target rather than E.

“The antibody binds NS1 in a manner that prevents NS1 from getting into sensitive human cells and mucking about with ordinary functions of the cell,” said Janet Smith, a professor in life sciences and biological chemistry at the University of Michigan, in an email.

Some implications of this study are that one region of NS1 could be the basis for developing a vaccine and that the antibody could be engineered to work as an antiviral drug, according to Smith. Her lab was able to identify which parts of NS1 interact with antibodies in “exquisite detail,” Smith added.

The study was “really collaborative,” as functional biologists, structural biologists and immunologists all worked together, according to Biering. Biering also noted that research on this topic will continue, and there are “a lot of different avenues to take.”