and since 2009 is professor of Human Immunology at the Swiss Federal Institute of Technology Zurich. Since January 2014 he had been appointed President of the Fondazione Regionale per la Ricerca Biomedica of the Region Lombardy, Italy.
US institutes and research centers receive thousands of francs from multinationals and banks. At risk is the independence of research and the educational freedom of students, unaware of everything ...
The investigation consulted the University of Italian Switzerland (Usi) on the matter.
Its members include the Biomedicine Research Institute (Irb), created in Bellinzona in 2000 and affiliated with the USI. The IRB deals with immunology, experimenting on human and animal cells: it is here that the first "human mouse" was created last April to try to fight Sida and Sars. Usi and Irb have close ties: the director of the scientific committee is the dean of the Ticino university, the immunologist Marco Baggiolini. The research is instead directed by the Italian Antonio Lanzavecchia.
But as industries and public institutions invest millions in biotechnology, citizens are sharing such research less and less. The issue is ethically controversial. Especially since the Swiss, in 1998, authorized the production and sale of genetically modified animals and plants.
The second important private funding comes from the third world biotech group, after the Americans Amgen and Genentech, the Geneva-based Serono, which already sponsors universities around the world. From this, the IRB has so far received 1.9 million francs, but has allocated 4.8 million until 2006 to promote the Ticino Biopolo. Its manager, Ernesto Bertarelli, sits on the board of directors of Ubs.
"Funding of this type is frequent in research institutes" replies to the Lanzavecchia Inquiry. "They are of mutual benefit and do not affect the freedom of research in the slightest," he adds
The aim is to support biotech in the canton, including by buying or selling patents.
GlaxoSmithKline (NYSE:GSK) is making a $250 million equity investment in Vir to gain access to its technology. As part of the agreement announced this month, the two companies will use Vir monoclonal antibody technology to identify anti-viral antibodies that could be used to treat or prevent coronavirus. The companies will move promising candidates into Phase 2 clinical trials within three to five months.
Structural Basis for Broad HIV-1 Neutralization by the MPER-Specific Human Broadly Neutralizing Antibody LN01
Georgia Tomaras David C Montefiori
Antonio Lanzavecchia
Lausanne University Hospital
University of Milan
Potent and broadly neutralizing antibodies (bnAbs) are the hallmark of HIV-1 protection by vaccination. The membrane-proximal external region (MPER) of the HIV-1 gp41 fusion protein is targeted by the most broadly reactive HIV-1 neutralizing antibodies. Here, we examine the structural and molecular mechansims of neutralization by anti-MPER bnAb, LN01, which was isolated from lymph-node-derived germinal center B cells of an elite controller and exhibits broad neutralization breadth. LN01 engages both MPER and the transmembrane (TM) region, which together form a continuous helix in complex with LN01. The tilted TM orientation allows LN01 to interact simultaneously with the peptidic component of the MPER epitope and membrane via two specific lipid binding sites of the antibody paratope. Although LN01 carries a high load of somatic mutations, most key residues interacting with the MPER epitope and lipids are germline encoded, lending support for the LN01 epitope as a candidate for lineage-based vaccine development.
A public antibody lineage that potently inhibits malaria infection through dual binding to the circumsporozoite protein
Immunization with attenuated Plasmodium falciparum sporozoites (PfSPZs) has been shown to be protective against malaria, but the features of the antibody response induced by this treatment remain unclear. To investigate this response in detail, we isolated IgM and IgG monoclonal antibodies from Tanzanian volunteers who were immunized with repeated injection of Sanaria PfSPZ Vaccine and who were found to be protected from controlled human malaria infection with infectious homologous PfSPZs. All isolated IgG monoclonal antibodies bound to P. falciparum circumsporozoite protein (PfCSP) and recognized distinct epitopes in its N terminus, NANP-repeat region, and C terminus. Strikingly, the most effective antibodies, as determined in a humanized mouse model, bound not only to the repeat region, but also to a minimal peptide at the PfCSP N-terminal junction that is not in the RTS,S vaccine. These dual-specific antibodies were isolated from different donors and were encoded by VH3-30 or VH3-33 alleles that encode tryptophan or arginine at position 52. Using structural and mutational data, we describe the elements required for germline recognition and affinity maturation. Our study provides potent neutralizing antibodies and relevant information for lineage-targeted vaccine design and immunization strategies.
Crystal structure and size-dependent neutralization properties of HK20, a human monoclonal antibody binding to the highly conserved heptad repeat 1 of gp41