Re:Search Institution Members

160 Results for Members


Established in 2013, University of Rwanda is committed to graduating the next generation of leaders who are...

The University of the Republic of Uruguay (UdelaR) is the main institution of higher education and research in...

The National Hansen's Disease Program (NHDP), part of the US Health Resources & Services Administration (HRSA)...

Anchor University Lagos (AUL) is a private, non-profit institution in Ayobo-Ipaja, Lagos, Nigeria. AUL’s...

171 Results for Collaborations


Parasitic worms cause substantial morbidity and mortality worldwide, and a heavy reliance on anti-parasitic treatments has led to drug resistance, with no effective vaccine available for most parasites. In order to address this high priority gap, the team of Professor Robin Gasser at the University of Melbourne has developed a high throughput whole-organism assay for anthelmintic drug discovery. Johnson & Johnson will provide its Jump-stARter library for screening in the assay.

Dr. Chiaka Anumudu at University of Ibadan previously identified 54 human proteins as potential biomarkers for schistosomiasis and bladder pathologies. Through WIPO Re:Search, Dr. Anumudu shared 60 urine samples with Dr. Horacio Bach at the University of British Columbia to support biomarker identification and validation. Upon identification of the biomarker(s), recombinant antibodies will be generated in Dr. Bach’s laboratory to develop a serological test for fast diagnosis.

Approximately 11,000 people per month die, and approximately 450,000 people per year suffer life-altering injuries such as amputation and permanent disability, due to snakebite envenoming. Professor Nicholas Casewell, a Wellcome Trust research fellow at the Centre of Snakebite Research and Interventions (CSRI), Liverpool School of Tropical Medicine, is working on innovative approaches to discover and develop the next generation of treatments for snakebites. To support these efforts, Johnson & Johnson will be sharing its diverse compound library and a targeted set of compounds to potentially identify novel inhibitors of the toxic components of snake venom.

Johnson & Johnson is sharing its Jump-stARter library with Dr. Peter Myler at Seattle Children’s Research Institute (SCRI) for screening for leishmaniasis drug discovery. Under the umbrella of the Seattle Structural Genomics Center for Infectious Disease, SCRI is partnering with the University of Washington’s Dr. Wes Van Voorhis to carry out the screening.

Dr. Stenio Fragoso, Head of the Laboratory of Molecular Biology of Trypanosomatids at Fundação Oswaldo Cruz (Fiocruz), is interested in testing inhibitors against recombinant T. cruzi Topoisomerase II. To initiate these studies, Dr. Fragoso and investigators from Seattle Children’s Research Institute (SCRI) and the National Institute of Allergy and Infectious Diseases (NIAID)-funded Seattle Structural Genomics Center for Infectious Disease (SSGCID; contract HHSN272201700059C) are collaborating to develop constructs to express and purify T. cruzi Topoisomerase II. Once the protein is purified, it will be incorporated into an in vitro assay to identify new drugs for Chagas disease.

Merck KGaA, Darmstadt, Germany will be sharing its Mini Library of compounds with Prof. Fabrice Boyom at University of Yaoundé I for leishmaniasis and amoebiasis drug discovery. Merck KGaA, Darmstadt, Germany’s Mini Library is a collection of drug-like former Biopharma research and development compounds and their derivatives. The compounds cover a wide range of molecular targets, including enzymes, hormone and neurotransmitter receptors, transporters, and ion channels.

171 Results for Assets


This invention comprises a number of novel anti-mycobacterial compositions, which offer to significantly improve the treatment of mycobacterial infection such as tuberculosis. These newly discovered anti-mycobacterial compounds, which are analogs of thiatetracosanoate, have been shown effective in the treatment of mycobacterial infections and are relatively nontoxic. They may be given alone or in combination with standard anti-mycobacterial drugs and are valuable as antiseptics as well as therapeutics.
DNA segments encoding the Duffy receptor of a Plasmodium parasite A useful protein in the development of a potential malaria vaccine has been developed by cloning the gene for the Duffy binding receptor of Plasmodium vivax, a human malaria. Duffy blood group determinants on human erythrocytes are known to be essential for invasion by both the P. vivax and P. knowlesi malaria strains. A candidate malaria vaccine could result from the use of antibodies to the recombinant Duffy receptor binding protein or the receptor protein itself functioning through competitive blocking therapy.
Pvs28, a vaccine candidate for blocking transmission of plasmodium vivax This invention relates to methods for preventing transmission using PVs28 polypeptide of malaria by eliciting an immune response against parasites responsible for the disease. The Pvs28 polypeptide which is isolated from Plasmodium vivax can be administered to a susceptible organism to prevent transmission of malaria. Claims in this application are drawn to the Pvs28 polypeptide, the nucleic acid molecule which encodes Pvs28, pharmaceutical compositions containing Pvs28, and methods of inducing an immune response against Pvs28.
Oligo- or poly Ci 1~2 -D-glucose-based vaccine for tuberculosis including pneumonia and all primary infections caused by Mycobacterium tuberculosis vaccine, synthetic or natural, that will induce poly a~1~2 -D-glucose antibodies with bactericidal activity against Mycobacterium tuberculosis. These antibodies by be achieved by a: parenteral administration of a vaccine containing a synthetic or a natural saccharide with poly a 1~2 -D-glucose or a structural related antigen. The oligo- or poly a 1~2 -D-glucose; as a natural or synthetic product, may be bound to a carried saccharide and then to a non-toxic non-host protein carrier by directly to a non-toxic non-host protein carrier to form a donjugate. The saccharide-based vaccines is planned for active immunization for prevention of tuberculosis and TIor preparation of immune antibodies as a therapy. The scope of the patent should be confined to this poly Ci 1~2 -D-glucose-based vaccine which is designed to confer specific preventative immunity to infection with Mycobacterium tuberculosis and to induce antibodies specific to poly a 1~2 -D-glucose for therapy of tuberculosis.
A fragment of the PfHRP-II gene of Plasmodium falciparum was cloned using recombinant DNA techniques. This clone is capable of encoding PfHRP-II protein, a water-soluble, histidine-rich molecule that may be effective in the detection, diagnosis, and treatment of human malaria, which is caused by the parasite, P. falciparum. This protein may be particularly useful in the development of an anti-malaria vaccine. To date, no malaria vaccine has been successful in human trials and most exhibit only limited effectiveness in primates. Recombinant DNA clone containing a genomic fragment of PfHRP-II gene from plasmodium falciparum The invention relates to isolated clones of DNA from Plasmodium falciparum that encode a histidine-rich protein from that organism. The PfHRPII protein is expressed in P. falciparum-infected erythrocytes. The cloned gene segment includes an intron-exon boundary near the amino-terminus of the coding sequence. The PfHRPII protein has a Mr of 60-80 kDa as determined by SDS-PAGE. This is substantially higher than the molecular weight of about 35 kDa as estimated from the predicted amino acid sequence of PfHRPII. The PfHRPII amino acid sequence includes a hydrophobic leader sequence, consistent with secretion of PfHRPII observed in vivo and in vivo. The amino acid sequence of PfHRPII is also characterized by a number of tandem repeats having a high content of histidine, alanine and aspartic acid.
Monoclonal antibodies (MABs) that block the transmission of malaria (Plasmodium falciparum or Plasmodium gallinaceum) to mosquitoes offer an improved method for controlling the spread of this disease. There has previously been no effective method of preventing mosquitoes for acquiring malarial parasites. These MABs, which block fertilization of the gametes preventing formation of the zygote and development of the zygote in the mosquito midgut, exhibit affinity and specificity for proteins located on the surface of the gametes or ookinetes of the malaria parasite.