Human-derived Monoclonal Antibody for Treatment of Ebola Virus Infection

Ebola virus infection can lead to severe hemorrhagic fever, known as Ebola virus disease (EVD), which is often fatal. The Zaire species of Ebola virus (EBOV) was responsible for the largest Ebola outbreak in history, which occurred in 2014. Scientists at the NIAID Vaccine Research Center have developed a human monoclonal neutralizing antibody, mAb114 for treatment and prevention of EBOV infection. Because there are very few treatments available to treat or prevent EBOV infection, there is a great need to develop effective pre- and post- exposure therapeutics before another outbreak occurs.

Recombinant Stabilized Prefusion Protein of Respiratory Syncytial Virus for Use as a Subunit Vaccine

The invention, a stabilized recombinant prefusion F protein (pre F), is a candidate subunit vaccine for Respiratory Syncytial Virus (RSV). Pre-F is stabilized in the prefusion conformation and displays epitopes not present in postfusion F protein. Several potent RSV neutralizing antibodies bind pre F, but not postfusion F. Therefore, immunization with pre F may elicit an immune response superior to the response generated by postfusion F.

Substitutions-Modified Prefusion RSV F Proteins and Their Use

The respiratory syncytial virus (RSV) fusion (F) glycoprotein is the primary target of neutralizing antibodies. The F glycoprotein exists in at least two conformations, a meta-stable prefusion state, and an extremely stable postfusion state. Both states share several epitopes targeted by neutralizing antibodies, but it has been demonstrated that the prefusion conformation of F contains at least one epitope not present in the postfusion conformation.

Fusion Glycoprotein Vaccine for Human Metapneumovirus

Human metapneumovirus (hMPV), a negative, single-stranded RNA virus, accounts for approximately 5-15% of infant respiratory tract infections and poses a severe risk of disease and hospitalization in both the elderly and the immunocompromised. Investigators at the Vaccine Research Center (VRC) of the National Institute of Allergy and Infectious Diseases (NIAID) have generated an hMPV fusion glycoprotein (“F protein”) stabilized in a prefusion conformation.

Prefusion-Stabilized Fusion (F) Glycoprotein Vaccine Immunogens For Human Metapneumovirus

Human metapneumovirus (hMPV) infections have been shown as a common cause of upper and lower respiratory diseases such as bronchiolitis and pneumonia in young children, the elderly, and other immunocompromised individuals. Studies show that infections by the non-segmented negative strand RNA virus begin with attachment and entry of viral glycoproteins that mediate fusion with host cellular membranes. Like for the human respiratory syncytial virus (hRSV), a viral entry is initiated by the fusion (F) protein.

Broadly neutralizing influenza hemagglutinin stem-directed antibodies

In 2023, the World Health Organization (WHO) reported roughly 3 to 5 million cases of severe influenza worldwide, resulting in approximately 290,000 to 650,000 deaths. Given the high disease burden, the needs for both prophylactic and therapeutic influenza strategies remain significant. However, current treatments for influenza are susceptible to resistance and are useful for only a limited post-infection period.    

Novel VAR2CSA Immunogens and Methods of Use Thereof

The invention provides immunogen polypeptides comprising fragments of VAR2CSA protein expressed by P. falciparum as potential second-generation placental malaria vaccine candidates. VAR2CSA is the leading antigen target for a placental malaria vaccine, where associated antibody titers are correlated with protection. Aspects of the inventive immunogen polypeptides comprise all or portions of the chondroitin sulfate A (CSA) binding regions of VAR2CSA, as identified by a structural study of VAR2CSA conducted by the inventors, that possess great sequence conservation among P.

Novel Compositions of Matter Comprising Stabilized Coronavirus Antigens and Their Use

Using a computational design methodology, SARS-CoV-2 spike proteins containing engineered amino acid changes to the receptor binding domain (RBD) were designed. These engineered spike proteins improved the immune response upon immunization of animals. An engineered RBD was also expressed at greater yield, had increased temperature stability, and improved the immune response upon immunization of animals. Specifically, the disclosed RBD designs can be produced approximately 7 times more efficiently than the native sequence, facilitating vaccine manufacturing on a global scale.

Enhanced Stability and Efficacy of Pfs48/45 Domain III Protein Variants for Malaria Vaccine Development Using SPEEDesign Technology

The technology includes modifying the Plasmodium falciparum Pfs48/45 Domain III protein sequence to enhance its stability and efficacy to aid in malaria vaccine development. This approach successfully overcomes previous production challenges by increasing the thermostability of the antigen and eliminating the need for additional modifications that could impair vaccine effectiveness. Crucially, the technology maintains the essential neutralizing epitope of Pfs48/45, ensuring its effectiveness in preventing malaria transmission as a transmission-blocking vaccine.

Next-Generation MSP1-Targeted Malaria Immunotherapy: Enhanced Vaccine Candidates and Monoclonal Antibodies

This technology encompasses the development of highly advanced malaria vaccine candidates and human monoclonal antibodies, both centered on targeting the Merozoite Surface Protein 1 (MSP1) of the Plasmodium falciparum malaria parasite. The innovation lies in utilizing a novel computational design and in vitro screening process, which has created MSP1 vaccine candidates that are significantly more immunogenic, stable, and cost-effective than existing alternatives. These vaccines focus on the 19 kDa carboxy-terminus fragment of MSP1.

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