Antibody therapeutics have transformed the treatment and prevention of infectious and immune-mediated diseases. Yet most remain limited by specificity: they target a single strain, a single epitope, or a single tumor antigen. However, through the identification of conserved molecular targets and structural optimization, scientists are developing antibodies that act broadly across viral variants, parasite species, and even tumor types, which we will refer to as universal antibodies.
A recent study led by the University of Cologne introduced the antibody 04_A06, which neutralized 98.5% of more than 300 HIV strains tested. Derived from “elite neutralizers”, which are individuals whose immune systems naturally suppress the virus, 04_A06 demonstrated not only exceptional breadth but also durable viral suppression in humanized mice.
Structural analysis revealed that the antibody possesses an unusually long amino acid chain capable of reaching conserved regions of the HIV envelope protein that are typically inaccessible to other antibodies. These regions are essential for viral function and difficult to mutate without compromising infectivity, explaining the antibody’s resistance to viral escape.

Researchers at The Jackson Laboratory, The University of Georgia, and the Scripps Research Institute reported a different but complementary strategy against influenza. Instead of relying on direct neutralization, their antibody cocktail engaged the immune system to clear infection by tagging infected cells. The therapy targeted a small, highly conserved region of the influenza A virus matrix protein (M2e), which remains stable across human, avian, and swine strains.
In mouse models, this antibody combination provided protection against nearly every strain tested, including avian and swine variants, without inducing viral escape even after repeated exposure. The study challenges the traditional view that only neutralizing antibodies are therapeutically useful, highlighting how non-neutralizing antibodies that leverage Fc-mediated effector functions can also achieve broad and durable protection.

At the University of Maryland School of Medicine, a first-in-human trial of the monoclonal antibody MAM01 demonstrated complete protection against malaria infection following exposure to infected mosquitoes. The antibody targets a highly conserved region of the Plasmodium falciparum circumsporozoite protein (CSP), blocking parasite entry into the bloodstream.
A single injection provided months of protection in healthy volunteers without notable side effects. The results confirm that targeting conserved parasite epitopes can yield long-lasting, strain-independent protection, thus offering an alternative to vaccines that require multiple doses and periodic boosters.
The principle of universal targeting is now extending into oncology. Researchers at Pohang University of Science and Technology have developed a “universal antibody” system, Univody, that enables immune recognition of tumors regardless of antigen type. The platform delivers genetic constructs that express antibody Fc fragments directly on the tumor surface, effectively converting any cancer cell into an immune target. In mouse models, Univody enhanced NK cell–mediated cytotoxicity and suppressed tumor growth across multiple cancer types.

Similarly, scientists at the UC Irvine designed a bispecific molecule termed GlyTR (glycan-dependent T-cell recruiter). This construct combines a lectin domain that binds tumor-associated glycans with a single-chain antibody that engages T cells. The multivalent “Velcro-like” interaction allows T cells to recognize and destroy cancer cells characterized by dense glycan patterns, which is a feature common to diverse solid tumors but absent in normal tissues.

Researchers in the field of antibody engineering are now moving towards designing molecules not limited by strain, species, or antigen type. From HIV and influenza to malaria and solid tumors, recent studies highlight a shared trend: focusing on conserved biological structures to achieve broad, escape-resistant efficacy.
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