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(12) INTERNATIONALAPPLICATION PUBLISHED UNDER THE PATENT COOPERATION TREATY (PCT) (19) World Intellectual Property Organization International Bureau (10) International Publication Number (43) International Publication Date 19 November 2009 (19.11.2009) WO 2009/140215 A2 (51) International Patent Classification: (74) Agents: BROWDY AND NEIMARK, P.L.L.C. et al; A61K 31/47 (2006.01) A61P 31/10 (2006.01) 624 Ninth Street N.W., Suite 300, Washington, DC A61P 31/04 (2006.01) A61K 31/435 (2006.01) 20001-5303 (US). (21) International Application Number: (81) Designated States (unless otherwise indicated, for every PCT/US2009/043505 kind of national protection available): AE, AG, AL, AM, AO, AT, AU, AZ, BA, BB, BG, BH, BR, BW, BY, BZ, (22) International Filing Date: CA, CH, CN, CO, CR, CU, CZ, DE, DK, DM, DO, DZ, 11 May 2009 ( 11.05.2009) EC, EE, EG, ES, FI, GB, GD, GE, GH, GM, GT, HN, (25) Filing Languag* English HR, HU, ID, IL, IN, IS, JP, KE, KG, KM, KN, KP, KR, KZ, LA, LC, LK, LR, LS, LT, LU, LY, MA, MD, ME, (26) Publication Language: English MG, MK, MN, MW, MX, MY, MZ, NA, NG, NI, NO, (30) Priority Data: NZ, OM, PG, PH, PL, PT, RO, RS, RU, SC, SD, SE, SG, 61/052,2 12 11 May 2008 ( 11.05.2008) US SK, SL, SM, ST, SV, SY, TJ, TM, TN, TR, TT, TZ, UA, 61/053,040 14 May 2008 (14.05.2008) US UG, US, UZ, VC, VN, ZA, ZM, ZW. 61/056,032 26 May 2008 (26.05.2008) us (84) Designated States (unless otherwise indicated, for every 61/056,077 27 May 2008 (27.05.2008) us kind of regional protection available): ARIPO (BW, GH, 61/057,1 17 29 May 2008 (29.05.2008) us GM, KE, LS, MW, MZ, NA, SD, SL, SZ, TZ, UG, ZM, 61/078,771 8 July 2008 (08.07.2008) us ZW), Eurasian (AM, AZ, BY, KG, KZ, MD, RU, TJ, 61/156,9 11 3 March 2009 (03.03.2009) us TM), European (AT, BE, BG, CH, CY, CZ, DE, DK, EE, 61/159,463 12 March 2009 (12.03.2009) us ES, FI, FR, GB, GR, HR, HU, IE, IS, IT, LT, LU, LV, 61/168,944 14 April 2009 (14.04.2009) us MC, MK, MT, NL, NO, PL, PT, RO, SE, SI, SK, TR), (71) Applicant (for SD only): GERAGHTY, Erin [US/US]; OAPI (BF, BJ, CF, CG, CI, CM, GA, GN, GQ, GW, ML, 6649 Cambria Terrace, Elkridge, MD 21075 (US). MR, NE, SN, TD, TG). (71) Applicant and Published: (72) Inventor: XILINAS, Michel, E . [FR/CY]; Stadiou 7, — without international search report and to be republished Aradippou, CY-7103 (CY). upon receipt of that report (Rule 48.2(g)) (54) Title: METHOD FOR TREATING DRUG-RESISTANT BACTERIAL AND OTHER INFECTIONS WITH CLIOQUINOL, PHANQUINONE, AND RELATED COMPOUNDS (57) Abstract: The invention relates to new uses of known chelating compounds for the treatment of bacterial in fungal infections, particularly by methicilllin-resistant and other drug-resistant strains of bacteria and fungi. One of more chelating compound is ad ministered with or without additional antibiotic or antifungal drugs to achieve improved therapy. Preferred chelating compounds include clioquinol, 5,7-dichloro-8-hydroxy-quinaldine, phanquinone, 5,7-dichloro-8-hydroxyquinoline, 5,7- di-iodo-8-hydrox- yquinoline. By chelation of specific metal ions, these compounds treat any infection by bacteria or fungi whose pathogenicity de pends upon metalloenzymes that require these cations. The compounds are also effective against infections caused by extended β lactamase and metallo β lactamase producing bacterial strains. Bacteria targeted by these methods include methicillin-resistant Staphylococcus aureus, penicillin resistant or intermediate resistant Streptococcus pneumoniae and other gram positive and mul- tiresistant gram negative species and strains. METHOD FOR TREATING DRUG-RESISTANT BACTERIAL AND OTHER INFECTIONS WITH CLIOQUINOL, PHANQUINONE, AND RELATED COMPOUNDS BACKGROUND OF THE INVENTION Field of the Invention The present invention relates to a new use of clioquinol, phanquinone, combinations thereof, or other chelating agents alone or in combination in the treatment of bacterial infections and infections with other organisms that are resistant to known antibiotics or antiinfective agents. Description of the Background Art Infections caused by multi-drug-resistant (MDR) bacteria are the result of ecological pressure exerted by the use and overuse of antibiotics, proving that the world of bacteria is an intelligent and difficult opponent. It has been disappointing to see the pharmaceutical industry stepping back from anti-infective R&D programs, because antibiotics are associated with low returns on investment. Approval of new antibacterial agents by the U.S. Food and Drug Administration (FDA) has fallen by 56% over the past 20 years. Furthermore, the regulatory approval rules represent a real hurdle that industry has to overcome, before launching a new agent onto the market. Legislative solutions, facilitating the development of new antimicrobial agents, are needed. In March 2003, the Infectious Diseases Society of America established the Antimicrobial Availability Task Force (AATF), which was responsible for ensuring future antibiotic availability through the evaluation of current trends and promotion of R&D programs. Multiple Drug Resistant (MDR) Bacteria as Causative agents in Serious Infection Gram-positive cocci, particularly Staphylococcus aureus, coagulase-negative staphylococci (CoNS) and Enterococcus spp., followed by Escherichia coli, Pseudomonas aeruginosa and Enterobacter spp., are the most commonly encountered pathogens in surgical site infections (SSIs) according to the National Nosocomial Infection Surveillance System reports. Although epidemiology changes over time and varies across different settings, as well as among different countries, there has been an increased prevalence of Gram-negative bacilli over time , which predominates among orthopedic and trauma patients as well as intensive care unit (ICU) surgical patients. In the latter case, P. aeruginosa is the most frequent pathogen present in SSI. Among out- patients and non-ICU surgical patients, S. aureus predominates, whereas an increased prevalence of Acinetobacter baumannii in SSI has been observed throughout Europe. It is easily concluded that the changing epidemiology has expanded in SSI the threat of all the highly problematic MDR pathogens, also identified as "AATF" : namely A. baumannii, extended- spectrum beta-lactamase (ESBL)-producing Enterobacteriaceae, P. aeruginosa, MRSA- and vancomycin-resistant Enterococcusfaecium (VREF). Due to their multiple inherent or acquired mechanisms of resistance that enable them to escape from antimicrobial agents, all these species have been implicated in the difficult-to-treat nosocomial infections. Bacterial enzymes Microbial proteases are predominantly extracellular enzymes that can be classified into four groups based on the essential catalytic residue at their active site. They include serine proteases (EC 3.4.21), cysteine proteases (also called thiol proteases) (EC 3.4.22), aspartate proteases (EC 3.4.23), and the metalloproteases (EC 3.4.24). Extracellular zinc-containing metalloproteases are widely distributed in the bacterial world (Hase CC & Finkelstein RA, Microbiol Rev. 1993 57:823-37). The most extensively studied are those which are associated either with pathogenic bacteria or industrially significant bacteria. They are found practically anywhere they are sought in both gram- negative and gram-positive microorganisms, be they aerobic or anaerobic. This ubiquity in itself implies that these enzymes serve important functions. Because of the importance of Zn to enzymatic activity, it is not surprising that there is a pervasive amino acid sequence homology among members of this family of enzymes regardless of their source. The evidence suggests that both convergent and divergent evolutionary forces are at work. Within the large family of bacterial Zn-containing metalloendopeptidases, smaller family units are observed, such as thermolysin-like, elastase-like, and Serratia protease-like metalloproteases from various bacterial species. More recently a new function for Zn-containing metalloproteases was discovered: the neurotoxins of Clostridium tetani and Clostridium botulinum type B are Zn metalloproteases with specificity for synaptobrevin, an integral membrane protein of small synaptic vesicles which is involved in neurotransmission. Most metalloproteases are Zn-containing proteins. Zn is an integral component of many proteins which are involved in virtually all aspects of metabolism of the different species of all phyla. In all Zn enzymes whose crystal structures are known, a catalytic Zn atom is coordinated to three amino acid residues and an active water molecule, whereas structural Zn atoms are coordinated to four Cys residues (Vallee, BL et al, 1990, Biochemistry 29:5647-59). A combination of His, GIu, Asp, or Cys residues creates a tridentate active Zn site, and an activated water molecule fills and completes the coordination sphere. Streptococcus pneumoniae (Pneumococci) Pneumococci display large Zn metalloproteinases on their surface, including the IgA protease, which cleaves human IgAl antibodies in the hinge region, the ZmpC proteinase, which cleaves human matrix metalloproteinase 9 (MMP-9), and two other proteinases, ZmpB and ZmpD, whose substrates have not yet been identified. Surface metalloproteinases are antigenic and have been linked to virulence. The genes encoding these proteinases reside in three distinct loci: two loci specific for zmpB and zmpC, and a third, the iga locus, containing iga and zmpD. The presence of the four proteinase genes is variable in the pneumococcal strains whose genomes have been sequenced. Studies of the presence of these genes in a collection of 218 pneumococcal isolates, mostly from invasive disease, (Camilli R et al. , Microbiology, 2006, 152(Pt 2):3 13-21) showed that zmpB and iga were present in all the isolates examined, while zmpC and zmpD were present in a variable proportions (18 and 49 %, respectively). Isolates carrying both zmpC and zmpD were found to belong mainly to two serotypes ("st's"), 8 and 1IA. By molecular typing, st 8 and st 1IA isolates appeared to belong to the same clonal cluster.
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    FINAL REPORT BioReD: Biomarkers and Tools for Reductive Dechlorination Site Assessment, Monitoring and Management SERDP Project ER-1586 November 2013 Frank Löffler Kirsti Ritalahti University of Tennessee Elizabeth Edwards University of Toronto Carmen Lebrón NAVFAC ESC Distribution Statement A This report was prepared under contract to the Department of Defense Strategic Environmental Research and Development Program (SERDP). The publication of this report does not indicate endorsement by the Department of Defense, nor should the contents be construed as reflecting the official policy or position of the Department of Defense. Reference herein to any specific commercial product, process, or service by trade name, trademark, manufacturer, or otherwise, does not necessarily constitute or imply its endorsement, recommendation, or favoring by the Department of Defense. Form Approved REPORT DOCUMENTATION PAGE OMB No. 0704-0188 Public reporting burden for this collection of information is estimated to average 1 hour per response, including the time for reviewing instructions, searching existing data sources, gathering and maintaining the data needed, and completing and reviewing this collection of information. Send comments regarding this burden estimate or any other aspect of this collection of information, including suggestions for reducing this burden to Department of Defense, Washington Headquarters Services, Directorate for Information Operations and Reports (0704-0188), 1215 Jefferson Davis Highway, Suite 1204, Arlington, VA 22202- 4302. Respondents should be aware that notwithstanding any other provision of law, no person shall be subject to any penalty for failing to comply with a collection of information if it does not display a currently valid OMB control number. PLEASE DO NOT RETURN YOUR FORM TO THE ABOVE ADDRESS.
  • The Genera Staphylococcus and Macrococcus

    The Genera Staphylococcus and Macrococcus

    Prokaryotes (2006) 4:5–75 DOI: 10.1007/0-387-30744-3_1 CHAPTER 1.2.1 ehT areneG succocolyhpatS dna succocorcMa The Genera Staphylococcus and Macrococcus FRIEDRICH GÖTZ, TAMMY BANNERMAN AND KARL-HEINZ SCHLEIFER Introduction zolidone (Baker, 1984). Comparative immu- nochemical studies of catalases (Schleifer, 1986), The name Staphylococcus (staphyle, bunch of DNA-DNA hybridization studies, DNA-rRNA grapes) was introduced by Ogston (1883) for the hybridization studies (Schleifer et al., 1979; Kilp- group micrococci causing inflammation and per et al., 1980), and comparative oligonucle- suppuration. He was the first to differentiate otide cataloguing of 16S rRNA (Ludwig et al., two kinds of pyogenic cocci: one arranged in 1981) clearly demonstrated the epigenetic and groups or masses was called “Staphylococcus” genetic difference of staphylococci and micro- and another arranged in chains was named cocci. Members of the genus Staphylococcus “Billroth’s Streptococcus.” A formal description form a coherent and well-defined group of of the genus Staphylococcus was provided by related species that is widely divergent from Rosenbach (1884). He divided the genus into the those of the genus Micrococcus. Until the early two species Staphylococcus aureus and S. albus. 1970s, the genus Staphylococcus consisted of Zopf (1885) placed the mass-forming staphylo- three species: the coagulase-positive species S. cocci and tetrad-forming micrococci in the genus aureus and the coagulase-negative species S. epi- Micrococcus. In 1886, the genus Staphylococcus dermidis and S. saprophyticus, but a deeper look was separated from Micrococcus by Flügge into the chemotaxonomic and genotypic proper- (1886). He differentiated the two genera mainly ties of staphylococci led to the description of on the basis of their action on gelatin and on many new staphylococcal species.