There is no vaccine for malaria, and there is growing resistance to existing anti-malarial drugs. Sexual stage-specific antigens are of interest as vaccine candidates because disruption of these antigens would reduce the fertility and, thus, the infectivity of the parasite.

The invention provides novel vectors, attenuated pathogens, compositions, methods and kits for preventing and/or treating chlamydia infections.

This technology describes the use of novel mutated anthrax protective antigen (PA) protein variants to target tumor cells and tumor vasculature. NIH scientists have engineered two PA variants that selectively complement one another and combine to form active octamers that target tumor cells. This controlled oligomeric activation of the PA proteins makes the likelihood of toxicity to non-tumor cells very low since non-tumor tissue does not express certain cell-surface proteases required to activate the PA variants.

This technology describes recombinant viruses that have weakened ability to establish and/or maintain latency and their use as live vaccines. The viruses have one or more genetic mutations that allow for continued replication but that inhibit latency. The vaccine materials and methods for their construction are exemplified with the virus that causes chickenpox and whose latent infection results in shingles, a condition that affects up to an estimated 1 million people per year in the United States alone. Additionally, there are veterinary applications of this technology.

Type I interferons play a critical role in both innate and adaptive immunity through the stimulation of the IFNAR1 which initiates interferon signaling in response to viral and bacterial infections. However, abnormal interferon signaling is associated with human diseases, such as lupus. The present invention discloses six hybridomas that produce mouse monoclonal antibodies specific for the extracellular domain of human IFNAR1. Two of the monoclonal antibodies are able to bind IFNAR1 and reduce interferon signaling.

Due to the disorganized nature of blood vessels that run through tumors, chemotherapeutic agents often fail to penetrate tumors and kill cancer cells at the tumor’s center. This can lead to ineffective chemotherapeutic treatments, because tumors can quickly grow back if the entire tumor is not destroyed. NIH researchers have developed a therapeutic agent that solves this problem facing current chemotherapy treatments.

Vaccines and therapies to prevent and treat Norovirus infections do not exist, despite the worldwide prevalence of Norovirus infections. Outbreaks of human gastroenteritis attributable to Norovirus commonly occur in group setting, such as hospitals, nursing homes, schools, dormitories, cruise ships and military barracks.

Strongyloides stercoralis is an intestinal nematode endemic that affects an estimated 30 to 100 million people worldwide. Many of these individuals may be asymptomatic for decades. The present invention discloses a NIE recombinant antigen that can be used in improved assays and diagnostics for S. stercoralis infection. The NIE antigen is the only one that is non-cross-reactive with sera from humans with other related filaria infections. The NIE antigen can be utilized as a skin test antigen for immediate hypersensitivity as well as for use in ELISA or other assays.

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.

This technology comprises sulfated recombinant gp120 proteins and peptides. Also included are methods for producing sulfated recombinant gp120 proteins. The focus of this technology is on sulfation of two tyrosines in the V2 loop of the HIV major envelope glycoprotein, gp120, which increase the stability of gp120 and promote the synthesis of gp120 protein in its native "closed" conformation. Gp120 in its native form is highly sulfated; however, recombinant gp120 produced for vaccines or structural analyses typically display low levels of V2 tyrosine sulfation.