Binding of hepatitis C virus to CD81.
- P. Pileri, Y. Uematsu, S. Abrignani
- Biology, MedicineScience
- 30 October 1998
Recombinant molecules containing this loop bound HCV and antibodies that neutralize HCV infection in vivo inhibited virus binding to CD81 in vitro.
The complete genome sequence of the Gram-positive bacterium Bacillus subtilis
- F. Kunst, N. Ogasawara, A. Danchin
- BiologyNature
- 20 November 1997
Bacillus subtilis is the best-characterized member of the Gram-positive bacteria, indicating that bacteriophage infection has played an important evolutionary role in horizontal gene transfer, in particular in the propagation of bacterial pathogenesis.
Genome analysis of multiple pathogenic isolates of Streptococcus agalactiae: implications for the microbial "pan-genome".
- H. Tettelin, V. Masignani, C. Fraser
- BiologyProceedings of the National Academy of Sciences…
- 27 September 2005
The genomic sequence of six strains representing the five major disease-causing serotypes of Streptococcus agalactiae, the main cause of neonatal infection in humans, was generated and Mathematical extrapolation of the data suggests that the gene reservoir available for inclusion in the S. agalactic pan-genome is vast and that unique genes will continue to be identified even after sequencing hundreds of genomes.
Complete genome sequence of Neisseria meningitidis serogroup B strain MC58.
- H. Tettelin, N. Saunders, J. Venter
- BiologyScience
- 10 March 2000
Neisseria meningitidis contains more genes that undergo phase variation than any pathogen studied to date, a mechanism that controls their expression and contributes to the evasion of the host immune system.
Identification of vaccine candidates against serogroup B meningococcus by whole-genome sequencing.
- M. Pizza, V. Scarlato, R. Rappuoli
- Biology, MedicineScience
- 10 March 2000
The entire genome sequence of a virulent serogroup B strain was used to identify vaccine candidates and allowed the identification of proteins that are surface exposed, that are conserved in sequence across a range of strains, and that induce a bactericidal antibody response, a property known to correlate with vaccine efficacy in humans.
Complete genome sequence and comparative genomic analysis of an emerging human pathogen, serotype V Streptococcus agalactiae
- H. Tettelin, V. Masignani, C. Fraser
- Biology, EngineeringProceedings of the National Academy of Sciences…
- 28 August 2002
In silico analyses, combined with comparative genome hybridization experiments between the sequenced serotype V strain 2603 V/R and 19 S. agalactiae strains from several serotypes using whole-genome microarrays, revealed the genetic heterogeneity among S. agriculture, provided insights into the evolution of virulence mechanisms.
Heterocyst Pattern Formation Controlled by a Diffusible Peptide
- S. Campagnoli, G. Galli, S. Abrignani
- Physics
- 1998
neglect transport through excited states. 11. The elastic current is given by the formula Iel(«) 5 eT c GR/[T c 2(2 1 GR/GL) 1 GR 2/4 1 («/h)2]; see Yu. V. Nazarov, Phys. B 189, 57 (1993); T. H.…
Group A Streptococcus produce pilus-like structures containing protective antigens and Lancefield T antigens
- M. Mora, G. Bensi, J. Telford
- Biology, MedicineProceedings of the National Academy of Sciences…
- 13 October 2005
It is reported that Group A Streptococcus, a Gram-positive human-specific pathogen that causes pharyngitis, impetigo, invasive disease, necrotizing fasciitis, and autoimmune sequelae has long, surface-exposed, pilus-like structures composed of members of a family of extracellular matrix-binding proteins.
CD81 extracellular domain 3D structure: insight into the tetraspanin superfamily structural motifs
- K. Kitadokoro, D. Bordo, M. Bolognesi
- BiologyEMBO Journal
- 15 January 2001
It is proposed that tetraspanins may assemble at the cell surface into homo‐ and/or hetero‐dimers through a conserved hydrophobic interface located in the stalk subdomain, while interacting with other liganding proteins, including hepatitis C virus E2, through the head subdomain.
Characterization and identification of vaccine candidate proteins through analysis of the group A Streptococcus surface proteome
- M. Rodríguez-Ortega, N. Norais, G. Grandi
- BiologyNature Biotechnology
- 1 February 2006
A proteomic approach for identifying bacterial surface-exposed proteins quickly and reliably for their use as vaccine candidates overcomes the difficulties so far encountered in surface protein characterization and has great potential in vaccine discovery.
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