SARAVIR

Science and data

Targeting a required step in measles virus entry

Saravir's antibodies are designed to interrupt the membrane-fusion step that measles virus requires to enter host cells.

Mechanism of action

Measles virus entry requires coordinated activity of its receptor-binding and fusion proteins. The fusion protein drives merger of the viral and cellular membranes. Saravir’s antibodies are designed to bind functionally important regions of the fusion protein and prevent the conformational changes required for viral entry.

Because protection is conferred by the administered antibody itself, it does not require the recipient to mount an immune response.

Measles entry mechanism. Left: the measles virus surface displays the H attachment protein bound to its cell receptor and the prefusion F protein. Without antibody, F extends into the host membrane and fusion proceeds so the virus enters. With a measles-specific antibody bound to F, fusion is blocked and no infection occurs.

Antibody discovery

The antibody program originated from human monoclonal antibody research at Vanderbilt University. Human monoclonal antibodies were isolated from previously infected individuals and evaluated for their ability to bind and neutralize measles virus.

Technology origin
Antibody research at Vanderbilt University Medical Center
Corporate rights
Exclusive license
Lead candidates
MEV-15 and MEV-104
Antibody source
Human monoclonal antibodies isolated from previously infected individuals

Preclinical evidence

Saravir's lead antibodies have been evaluated in binding, neutralization, breadth, escape-selection, and animal protection studies. Detailed assay-by-assay results are summarized in the non-confidential company overview.
More information

Resistance

No escape variants resistant to the antibody combination were detected under the in vitro selection conditions tested to date. Escape mutants selected against one lead antibody remained susceptible to the other.

The antibody combination is designed to increase the barrier to viral escape by targeting nonoverlapping conserved epitopes. These are in vitro observations under defined conditions and do not establish that resistance cannot emerge.

A manuscript describing the lead antibodies is currently under review.