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Tiny Antibody From Alpaca Blocks Two Deadly Viruses

Scientists have discovered a powerful new weapon against two of the world’s most lethal viruses—and it comes from an unlikely source.

A nanobody isolated from an alpaca named Pedro can neutralize both Nipah and Hendra viruses, which kill up to 100% of infected people and have no approved treatments. The finding offers hope for combating future pandemic threats from these emerging pathogens.

The nanobody, called DS90, represents just one-tenth the size of a traditional antibody yet demonstrates extraordinary potency against henipaviruses. Researchers at the University of Queensland and Universidad Austral de Chile used advanced imaging techniques to reveal how DS90 penetrates deep into viral proteins, reaching areas that conventional antibodies cannot access.

Alpaca Immunity Meets Human Medicine

“A nanobody is one-tenth the size of an antibody and being that small it can access hard-to-reach areas of a virus to block infection,” explained Dr. Ariel Isaacs, who led the University of Queensland study. “Nanobodies are also easier to produce and more stable at higher temperatures than traditional antibodies, so we are very excited about the potential of our discovery to lead to new treatments.”

Camelids—including alpacas, llamas, and camels—are the only land animals that naturally produce these ultracompact antibodies. Pedro the alpaca was immunized with Nipah virus proteins, allowing researchers to harvest nanobodies from his immune cells using a specialized platform developed by Professor Alejandro Rojas-Fernandez.

Cryogenic electron microscopy revealed DS90’s unique mechanism of action: the nanobody binds to a previously undiscovered pocket spanning multiple domains of the viral fusion protein, effectively locking the virus in an inactive state. This represents the first demonstration of quantum-level viral neutralization in three-dimensional henipavirus structures.

Preventing Viral Evolution

Perhaps most significantly, the team engineered a dual-targeting therapy that combines DS90 with m102.4, an experimental antibody currently in development for henipavirus treatment. This bispecific approach offers several advantages:

  • Prevents viral escape mutations by targeting two different proteins simultaneously
  • Provides 38-fold better neutralization than existing treatments against some viral strains
  • Demonstrates complete protection in animal challenge studies
  • Activates additional immune responses beyond neutralization

Laboratory evolution experiments confirmed the dual therapy’s resistance to viral escape. While viruses rapidly developed resistance to single antibodies within three passages, the DS90-m102.4 combination prevented any high-prevalence mutations from emerging.

Targeting a Growing Threat

Nipah virus outbreaks occur almost annually in Bangladesh, with occasional spillovers in India and the Philippines. Hendra virus has infected people through horses in eastern Australia since its discovery in Brisbane in 1994. Both viruses originate in fruit bats and can cause severe respiratory symptoms progressing to fatal encephalitis.

The nanobody’s thermal stability and production advantages make it particularly suitable for outbreak response in resource-limited settings. Unlike conventional antibodies requiring refrigeration, DS90 could potentially be delivered via inhalation or stored at ambient temperatures—critical features for rapid deployment during emergencies.

Structural analysis revealed that DS90 binds to highly conserved regions shared between Nipah and Hendra viruses, explaining its cross-protective activity. The binding site overlaps with regions important for the virus’s membrane fusion machinery, effectively disabling the infection process.

From Research to Reality

The research team has already begun humanizing DS90’s sequence to enable clinical translation. Initial humanization attempts reduced binding affinity, but strategic modifications based on the structural data restored full activity while maintaining human compatibility.

Professor Rojas-Fernandez emphasized the broader implications: “Together with UQ, we aimed to construct a broad barrier against future pandemic viruses based on scalable antiviral nanobodies—this fantastic work is just the beginning.”

The nanobody platform could potentially be adapted for other emerging viral threats, offering a rapid response capability for future pandemic preparedness. With other nanobodies already approved for cancer treatment, the regulatory pathway for antiviral applications appears increasingly feasible.

The next step involves translating these laboratory findings into a therapeutic ready for clinical testing, potentially providing the first effective treatment against henipaviruses that continue to threaten global health security.


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