The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
Gene Review

ftsI  -  penicillin-binding protein 3

Haemophilus influenzae Rd KW20

 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of ftsI

  • Cefuroxime resistance in non-beta-lactamase Haemophilus influenzae is linked to mutations in ftsI [1].
  • OBJECTIVES: To study yearly changes in resistance and to identify ftsI mutations in beta-lactamase-non-producing ampicillin-resistant (BLNAR) and TEM-1 beta-lactamase-producing amoxicillin/clavulanic acid-resistant (BLPACR) isolates of Haemophilus influenzae from patients with meningitis [2].
  • MATERIAL AND METHODS: We investigated mutations in the ftsI gene encoding PBP-3 of H. influenzae isolated from the nasopharynx of children with acute otitis media (AOM) using polymerase chain reaction (PCR) [3].
 

High impact information on ftsI

 

Chemical compound and disease context of ftsI

 

Biological context of ftsI

 

Associations of ftsI with chemical compounds

  • The transformation of H. influenzae Rd strain with amplified ftsI genes from two BLPACR and two BLNAR strains enabled the selection of amoxicillin/clavulanate-resistant transformants with the same mutations as their parent strains [8].
  • The MICs of cephalosporin antibiotics for H. influenzae transformants into which the ftsI genes from BLNAR strains of each of the nine subgroups were introduced increased to varying degrees depending on the mutations [2].
  • Strains without mutations in the ftsI gene and that did not contain the bla gene (non-beta-lactamase-producing ampicillin-susceptible) were identified in 70.7% of cases [3].

References

  1. Cefuroxime resistance in non-beta-lactamase Haemophilus influenzae is linked to mutations in ftsI. Straker, K., Wootton, M., Simm, A.M., Bennett, P.M., MacGowan, A.P., Walsh, T.R. J. Antimicrob. Chemother. (2003) [Pubmed]
  2. High prevalence of type b beta-lactamase-non-producing ampicillin-resistant Haemophilus influenzae in meningitis: the situation in Japan where Hib vaccine has not been introduced. Hasegawa, K., Kobayashi, R., Takada, E., Ono, A., Chiba, N., Morozumi, M., Iwata, S., Sunakawa, K., Ubukata, K. J. Antimicrob. Chemother. (2006) [Pubmed]
  3. Evaluation of mutations in penicillin binding protein-3 gene of non-typeable Haemophilus influenzae isolated from the nasopharynx of children with acute otitis media. Sakai, A., Hotomi, M., Billal, D.S., Yamauchi, K., Shimada, J., Tamura, S., Fujihara, K., Yamanaka, N. Acta Otolaryngol. (2005) [Pubmed]
  4. Molecular evolution of beta-lactam-resistant Haemophilus influenzae: 9-year surveillance of penicillin-binding protein 3 mutations in isolates from Japan. Sanbongi, Y., Suzuki, T., Osaki, Y., Senju, N., Ida, T., Ubukata, K. Antimicrob. Agents Chemother. (2006) [Pubmed]
  5. Genetic approach to study the relationship between penicillin-binding protein 3 mutations and Haemophilus influenzae beta-lactam resistance by using site-directed mutagenesis and gene recombinants. Osaki, Y., Sanbongi, Y., Ishikawa, M., Kataoka, H., Suzuki, T., Maeda, K., Ida, T. Antimicrob. Agents Chemother. (2005) [Pubmed]
  6. In vitro activity of Bay v 3522, a new cephalosporin, compared with activities of other agents. Wise, R., Andrews, J.M., Ashby, J.P., Thornber, D. Antimicrob. Agents Chemother. (1990) [Pubmed]
  7. Association of amino acid substitutions in penicillin-binding protein 3 with beta-lactam resistance in beta-lactamase-negative ampicillin-resistant Haemophilus influenzae. Ubukata, K., Shibasaki, Y., Yamamoto, K., Chiba, N., Hasegawa, K., Takeuchi, Y., Sunakawa, K., Inoue, M., Konno, M. Antimicrob. Agents Chemother. (2001) [Pubmed]
  8. Contribution of beta-lactamase and PBP amino acid substitutions to amoxicillin/clavulanate resistance in beta-lactamase-positive, amoxicillin/clavulanate-resistant Haemophilus influenzae. Matic, V., Bozdogan, B., Jacobs, M.R., Ubukata, K., Appelbaum, P.C. J. Antimicrob. Chemother. (2003) [Pubmed]
 
WikiGenes - Universities