title: Quinine specifically inhibits the proteolipid subunit of the F0F1 H+ -ATPase of Streptococcus pneumoniae.
abstract: Streptococcus pneumoniae is uniquely sensitive to quinine and its derivatives, but only those alkaloids having antimalarial properties, i.e., those in the erythro configuration, also possess antipneumococcal activity. Quinine and related compounds inhibit the pneumococcal H+ -ATPase. Quinine- and optochin-resistant pneumococci showed mutations that change amino acid residues located in one of the two transmembrane alpha-helices of the c subunit of the F0F1, H+ -ATPase.
authors.affiliation: Centro Nacional de Biología Celular y Retrovirus, Instituto de Salud Carlos III, Majadahonda, Spain.
authors.forename: R
authors.initials: R
authors.lastname: Muñoz
authors.forename: E
authors.initials: E
authors.lastname: García
authors.forename: A G
authors.initials: AG
authors.lastname: De la Campa
mesh_terms: D000595:Amino Acid Sequence; D000962:Antimalarials / Q000494:pharmacology*; D001483:Base Sequence; D004305:Dose-Response Relationship, Drug; D004352:Drug Resistance, Microbial; D004791:Enzyme Inhibitors / Q000494:pharmacology*; D008969:Molecular Sequence Data; D011510:Proteolipids / Q000037:antagonists & inhibitors*; D006180:Proton-Translocating ATPases / Q000037:antagonists & inhibitors*; D011803:Quinine / Q000031:analogs & derivatives / Q000494:pharmacology*; D013237:Stereoisomerism; D013296:Streptococcus pneumoniae / Q000201:enzymology*
chemical_list: D000962:Antimalarials; D004791:Enzyme Inhibitors; D011510:Proteolipids; C017303:ethylhydrocupreine; D011803:Quinine; D006180:Proton-Translocating ATPases