Robert A Bonomo

Case Western Reserve University School of Medicine, Cleveland, Ohio, United States

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Publications (357)1525.81 Total impact

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    ABSTRACT: We investigate the evolving molecular epidemiology of metallo-β-lactamase (MBL)-producing Pseudomonas aeruginosa isolates collected in a 100 institution, nationwide surveillance study in Japan from 2004 to 2006. MBL-producers were detected in 23/996 isolates (2.3%) in 2004 and 21/992 (2.1%) in 2006. Antimicrobial resistance (specifically, carbapenem resistance) rates between two periods did not differ significantly. MBL-producers were more prevalent in urinary tract isolates. bla IMP-1 group was the most predominant (38 isolates, 80%), followed by 3 bla IMP-7, 2 bla IMP-11 group, and 1 bla VIM-1. All MBL genes were identified in 16 different class 1 integrons, most of which were novel to INTEGRALL database. A total of 17 isolates of sequence type (ST) 235, a recognized worldwide drug-resistant lineage, were distributed in 5 geographic regions across Japan. ST235 isolates included a sublineage associated with In113-like integron. ST357 was identified in 14 isolates, 9 of which harboring a sole bla IMP-1 gene cassette (In994) were recovered from Chugoku region in 2004. ST357 isolates with bla IMP-11 group or ST235 with bla IMP-7 emerged in 2006. We also report for the first time the presence of novel fosI gene cassette in strains other than Mycobacterium spp. Our data give an important "snapshot" of the molecular characteristics and dynamics of MBL-producing lineages in P. aeruginosa in Japan. The significant association of specific genotypes and integrons implies that dissemination and transmission of the preexisting resistant lineage, rather than horizontal gene transfer in situ, might largely explain their endemicity.
    BMC Microbiology 12/2015; 15(1). DOI:10.1186/s12866-015-0378-8 · 2.98 Impact Factor
  • Brad Spellberg, Robert A Bonomo
    Critical care medicine 06/2015; 43(6):1332-1334. DOI:10.1097/CCM.0000000000001029 · 6.15 Impact Factor
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    ABSTRACT: OBJECTIVE To determine the rates of and risk factors for tigecycline nonsusceptibility among carbapenem-resistant Klebsiella pneumoniae (CRKPs) isolated from hospitalized patients DESIGN Multicenter prospective observational study SETTING Acute care hospitals participating in the Consortium on Resistance against Carbapenems in Klebsiella pneumoniae (CRaCKle) PATIENTS A cohort of 287 patients who had CRKPs isolated from clinical cultures during hospitalization METHODS For the period from December 24, 2011 to October 1, 2013, the first hospitalization of each patient with a CRKP during which tigecycline susceptibility for the CRKP isolate was determined was included. Clinical data were entered into a centralized database, including data regarding pre-hospital origin. Breakpoints established by the European Committee on Antimicrobial Susceptibility Testing (EUCAST) were used to interpret tigecycline susceptibility testing. RESULTS Of 287 patients included in the final cohort, 155 (54%) had tigecycline-susceptible CRKPs. Of all index isolates, 81 (28%) were tigecycline-intermediate and 51 (18%) were tigecycline resistant. In multivariate modeling, independent risk factors for tigecycline nonsusceptibility were (1) admission from a skilled nursing facility (OR, 2.51; 95% CI, 1.51-4.21; P=.0004), (2) positive culture within 2 days of admission (OR, 1.82; 95% CI, 1.06-3.15; P=.03), and (3) receipt of tigecycline within 14 days (OR, 4.38, 95% CI, 1.37-17.01, P=.02). CONCLUSIONS In hospitalized patients with CRKPs, tigecycline nonsusceptibility was more frequently observed in those admitted from skilled nursing facilities and occurred earlier during hospitalization. Skilled nursing facilities are an important target for interventions to decrease antibacterial resistance to antibiotics of last resort for treatment of CRKPs. Infect Control Hosp Epidemiol 2015;00(0):1-7.
    Infection Control and Hospital Epidemiology 05/2015; DOI:10.1017/ice.2015.118 · 3.94 Impact Factor
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    ABSTRACT: Innate defense regulator peptide-1018 (IDR-1018) is a 12-amino acid, synthetic, immunomodulatory host defense peptide that can reduce soft tissue infections and is less likely to induce bacterial resistance than conventional antibiotics. However, IDRs have not been tested on orthopaedic infections and the immunomodulatory effects of IDR-1018 have only been characterized in response to lipopolysacharide, which is exclusively produced by Gram-negative bacteria. We sought (1) to more fully characterize the immunomodulatory effects of IDR-1018, especially in response to Staphylococcus aureus; and (2) to determine whether IDR-1018 decreases S aureus infection of orthopaedic implants in mice and thereby protects the implants from failure to osseointegrate. In vitro effects of IDR-1018 on S aureus were assessed by determining minimum inhibitory concentrations in bacterial broth without and with supplementation of physiologic ion levels. In vitro effects of IDR-1018 on macrophages were determined by measuring production of monocyte chemoattractant protein-1 (MCP-1) and proinflammatory cytokines by enzyme-linked immunosorbent assay. In vivo effects of IDR-1018 were determined in a murine model of S aureus implant infection by quantitating bacterial burden, macrophage recruitment, MCP-1, proinflammatory cytokines, and osseointegration in nine mice per group on Day 1 postimplantation and 20 mice per group on Day 15 postimplantation. IDR-1018 demonstrated antimicrobial activity by directly killing S aureus even in the presence of physiologic ion levels, increasing recruitment of macrophages to the site of infections by 40% (p = 0.036) and accelerating S aureus clearance in vivo (p = 0.008) with a 2.6-fold decrease in bacterial bioburden on Day 7 postimplantation. In vitro immunomodulatory activity of IDR-1018 included inducing production of MCP-1 in the absence of other inflammatory stimuli and to potently blunt excess production of proinflammatory cytokines and MCP-1 induced by lipopolysaccharide. Higher concentrations of IDR-1018 were required to blunt production of proinflammatory cytokines and MCP-1 in the presence S aureus. The largest in vivo immunomodulatory effect of IDR-1018 was to reduce tumor necrosis factor-α levels induced by S aureus by 60% (p = 0.006). Most importantly, IDR-1018 reduced S aureus-induced failures of osseointegration by threefold (p = 0.022) and increased osseointegration as measured by ultimate force (5.4-fold, p = 0.033) and average stiffness (4.3-fold, p = 0.049). IDR-1018 is potentially useful to reduce orthopaedic infections by directly killing bacteria and by recruiting macrophages to the infection site. These findings make IDR-1018 an attractive candidate to explore in larger animal models to ascertain whether its effects in our in vitro and mouse experiments can be replicated in more clinically relevant settings.
    Clinical Orthopaedics and Related Research 05/2015; DOI:10.1007/s11999-015-4301-2 · 2.88 Impact Factor
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    ABSTRACT: The objective of this study was to explore the activity of ceftazidime and ceftazidime/avibactam against a collection of isogenic strains of Escherichia coli DH10B possessing SHV and KPC β-lactamases containing single amino acid substitutions in the Ω-loop (residues 164-179). Ceftazidime and ceftazidime/avibactam MICs were determined by the agar dilution method for a panel of isogenic E. coli strains expressing SHV-1 and KPC-2 with amino acid substitutions at positions 164, 167, 169 or 179. Two KPC-2 β-lactamase variants that possessed elevated MICs of ceftazidime/avibactam were selected for further biochemical analyses. Avibactam restored susceptibility to ceftazidime for all Ω-loop variants of SHV-1 with MICs <8 mg/L. In contrast, several of the Arg164 and Asp179 variants of KPC-2 demonstrated MICs of ceftazidime/avibactam >8 mg/L. β-Lactamase kinetics showed that the Asp179Asn variant of KPC-2 demonstrated enhanced kinetic properties against ceftazidime. The Ki app, k2/K and koff of the Arg164Ala and Asp179Asn variant KPC-2 β-lactamases indicated that avibactam effectively inhibited these enzymes. Several KPC-2 variants demonstrating ceftazidime resistance as a result of single amino acid substitutions in the Ω-loop were not susceptible to ceftazidime/avibactam (MICs >8 mg/L). We hypothesize that this observation is due to the stabilizing interactions (e.g. hydrogen bonds) of ceftazidime within the active site of variant β-lactamases that prevent avibactam from binding to and inhibiting the β-lactamase. As ceftazidime/avibactam is introduced into the clinic, monitoring for new KPC-2 variants that may exhibit increased ceftazidime kinetics as well as resistance to this novel antibiotic combination will be important. Published by Oxford University Press on behalf of the British Society for Antimicrobial Chemotherapy 2015. This work is written by (a) US Government employee(s) and is in the public domain in the US.
    Journal of Antimicrobial Chemotherapy 05/2015; DOI:10.1093/jac/dkv094 · 5.44 Impact Factor
  • Emerging infectious diseases 05/2015; 21(5). DOI:10.3201/eid2105.142033 · 7.33 Impact Factor
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    ABSTRACT: Acinetobacter-positive patients had their ambient air tested for up to 10 consecutive days. The air was Acinetobacter-positive an average of 21% of days; contamination was higher among patients colonized in the rectum than airways (RR, 2.35; p=0.006). Of 6 air/clinical isolate pairs available, four pairs were closely related using rep-PCR. Copyright © 2015, American Society for Microbiology. All Rights Reserved.
    Journal of clinical microbiology 04/2015; DOI:10.1128/JCM.00198-15 · 4.23 Impact Factor
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    ABSTRACT: β-lactamase inhibitors (BLIs) restore the efficacy of otherwise obsolete β-lactams. However, commercially available BLIs are not effective against metallo-β-lactamases (MBLs), which continue to disseminate globally. One of the most clinically important MBLs are the VIM family. The discovery of VIM-24, a natural variant of VIM-2, possessing an R228L substitution and a novel phenotype, compelled us to explore the role of this position and its effects on substrate specificity. We employed mutagenesis, biochemical and biophysical assays, and crystallography. VIM-24 (R228L) confers enhanced resistance to cephems and increases turnover compared to VIM-2 (kcat/KM increased by six to ten fold for ceftazidime and cefepime, respectively). Likely the R⇒L substitution relieves steric clashes and accommodates the C3N-methyl pyrrolidine group of cephems. Four novel bisthiazolidine (BTZ) inhibitors were next synthesized and tested against these MBLs. These inhibitors inactivated VIM-2 and VIM-24 equally well (Ki* 40 - 640 nM) through a two-step process wherein an initial enzyme (E) -inhibitor (I) complex (EI) undergoes a conformational transition to a more stable species, E*I. As both, VIM-2 and VIM-24 were inhibited in a similar manner, the crystal structure of a VIM-2:BTZ complex was determined at 1.25 Å and revealed interactions of the inhibitor thiol with the VIM Zn center. Most importantly, BTZs also restored the activity of imipenem against Klebsiella pneumoniae and Pseudomonas aeruginosa in whole cell assays producing VIM-24 and VIM-2, respectively. Our results suggest a role for position 228 in defining the substrate specificity of VIM MBLs, and show that BTZs inhibitors are not affected by the R228L substitution.
    Biochemistry 04/2015; DOI:10.1021/acs.biochem.5b00106 · 3.19 Impact Factor
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    ABSTRACT: RNase P is a ribozyme originally identified for its role in maturation of tRNAs by cleavage of precursor tRNAs (pre-tRNAs) at the 5'-end termini. RNase P is a ribonucleoprotein consisting of a catalytic RNA molecule and, depending on the organism, one or more cofactor proteins. The site of cleavage of a pre-tRNA is identified by its tertiary structure; and any RNA molecule can be cleaved by RNase P as long as the RNA forms a duplex that resembles the regional structure in the pre-tRNA. When the antisense sequence that forms the duplex with the strand that is subsequently cleaved by RNase P is in a separate molecule, it is called an external guide sequence (EGS). These fundamental observations are the basis for EGS technology, which consists of inhibiting gene expression by utilizing an EGS that elicits RNase P-mediated cleavage of a target mRNA molecule. EGS technology has been used to inhibit expression of a wide variety of genes, and may help development of novel treatments of diseases, including multidrug-resistant bacterial and viral infections. © 2015 New York Academy of Sciences.
    Annals of the New York Academy of Sciences 04/2015; DOI:10.1111/nyas.12755 · 4.31 Impact Factor
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    ABSTRACT: Whole genome sequencing (WGS) of large isolate collections has many applications, yet sequencing costs are still significant. We sought to develop a rapid and cost efficient WGS method to address fundamental questions in clinical microbiology. We evaluated the performance of SISPA (Sequence-Independent, Single-Primer Amplification) combined with next-generation sequencing (SISPA-Seq) of 75 clinical isolates of Acinetobacter baumannii to establish whether SISPA-Seq resulted in sufficient coverage and quality to 1) determine strain phylogenetic placement and 2) and carriage of known antibiotic resistance (AbR) genes. Strains for which whole genome sequences were available were included for validation. Two libraries for each strain were constructed from separate SISPA reactions with different barcoded primers, using genomic DNA prepared from either high quality or rapid heat-lysis preparations. SISPA-Seq resulted in a median of 65x genome coverage when reads from both primer sets were combined. Coverage and quality were sufficient for detection of AbR genes by comparison of reads to the ARG-ANNOT database and were often sufficient to distinguish between different allelic variants of the same gene. kSNP and RAxML were used to construct a robust phylogeny based on single-nucleotide variants (SNVs) that showed that the SISPA-seq data was sufficient for sensitive and accurate phylogenetic placement. Advantages of the SISPA-Seq method include inexpensive and rapid DNA preparation and a typical total cost less than one-half that of standard genome sequencing. In summary, SISPA-Seq can be used to survey whole genomes of a large strain collection and identify strains that should be targeted for additional sequencing. Copyright © 2015. Published by Elsevier B.V.
    Infection, genetics and evolution: journal of molecular epidemiology and evolutionary genetics in infectious diseases 03/2015; 32. DOI:10.1016/j.meegid.2015.03.018 · 3.26 Impact Factor
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    ABSTRACT: Among the 2105 Enterobacteriaceae tested in a survey done in Portugal, 165 were non-susceptible to carbapenems, from which 35 (26 Klebsiella pneumoniae, 3 Escherichia coli, 2 Enterobacter aerogenes, 3 Enterobacter cloacae and 1 Klebsiella oxytoca) were confirmed to be carbapenemase-producers, by the presence of 30 Tn4401d-blaKPC-3, 4 intI3-blaGES-5 and one intI1-blaVIM-2, alone or in combination with other bla genes. The dissemination of blaKPC-3 gene carried by an IncF plasmid suggests lateral gene transfer as a major mechanism of dissemination. Copyright © 2015, American Society for Microbiology. All Rights Reserved.
    Antimicrobial Agents and Chemotherapy 03/2015; DOI:10.1128/AAC.05065-14 · 4.45 Impact Factor
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    ABSTRACT: Horizontal transfer of blaKPC-harboring plasmids contributes significantly to the inter- and intra-species spread of Klebsiella pneumoniae carbapenemase (KPC). Here we report the complete nucleotide sequence of a blaKPC-harboring IncFIA plasmid, pBK32533 from Escherichia coli. pBK32533 is a co-integrate plasmid comprising of a 72-kb sequence identical to the non-conjugative pBK30661 plus an additional 170-kb element that harbors the genes for plasmid transfer. pBK32533 demonstrates how blaKPC can be spread from a non-conjugative plasmid through co-integration. Copyright © 2015, American Society for Microbiology. All Rights Reserved.
    Antimicrobial Agents and Chemotherapy 03/2015; 59(5). DOI:10.1128/AAC.00041-15 · 4.45 Impact Factor
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    ABSTRACT: The carbapenem-hydrolyzing class D β-lactamases OXA-23 and OXA-24/40 have emerged world-wide as causative agents for β-lactam antibiotic resistance in Acinetobacter species. Many variants of these enzymes have appeared clinically, including OXA-160 and OXA-225, which both contain a P→S substitution at homologous positions in the OXA-24/40 and OXA-23 backgrounds respectively. We purified OXA-160 and OXA-225 and used steady-state kinetic analysis to compare the substrate profiles of these variants to their parental enzymes, OXA-24/40 and OXA-23. OXA-160 and OXA-225 possess greatly enhanced hydrolytic activities against aztreonam, ceftazidime, cefotaxime and ceftriaxone when compared to OXA-24/40 and OXA-23. These enhanced activities are the result of much lower Km values, suggesting that the P→S substitution enhances the binding affinity of these drugs. We have determined the structures of the acylated forms of OXA-160 (with ceftazidime and aztreonam) and OXA-225 (ceftazidime). These structures show that the R1 oxyimino side-chain of these drugs occupies a space near the β5-β6 loop and the omega loop of the enzymes. The P→S substitution found in OXA-160 and OXA-225 results in a deviation of the β5-β6 loop, relieving the steric clash with the R1 side-chain carboxypropyl group of aztreonam and ceftazidime. These results reveal worrying trends in the enhancement of substrate spectrum of class D β-lactamases, but may also provide a map for β-lactam improvement.
    Biochemistry 02/2015; 54(10). DOI:10.1021/bi501547k · 3.19 Impact Factor
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    ABSTRACT: β-Lactamase enzymes (E.C.3.5.2.6) are a significant threat to the continued use of β-lactam antibiotics to treat infections. A novel non-β-lactam β-lactamase inhibitor, avibactam, is being developed with activity against many β-lactamase variants. Here, we explore the activity of avibactam (a diazabicyclooctane) against bacteria containing a variety of characterized isogenic laboratory constructs of β-lactamase inhibitor resistant variants of the class A enzyme SHV. We find that the S130G variant of SHV shows significant resistance to inhibition by avibactam by both microbiological and biochemical characterization. Our analysis leads us to hypothesize that the lack of a hydroxyl group at the 130 position in the S130G variant of SHV-1 slows carbamylation of the enzyme by avibactam. Thus, the S130G substitution is a common "key residue" for the inhibition of class A β-lactamases, perhaps even for the novel diazabicyclooctane class of β-lactamase inhibitors. Copyright © 2015, American Society for Microbiology. All Rights Reserved.
    Antimicrobial Agents and Chemotherapy 02/2015; DOI:10.1128/AAC.04405-14 · 4.45 Impact Factor
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    ABSTRACT: Avibactam is a novel β-lactamase inhibitor that restores the activity of otherwise hydrolyzed β-lactams against Gram-negative bacteria expressing different classes of serine β-lactamases. In the last decade, β-lactam-avibactam combinations were tested against a variety of clinical isolates expressing multiple commonly encountered β-lactamases. Here, we analyzed isogenic Escherichia coli strains expressing selected single β-lactamase genes that were not previously tested or were not characterized in an isogenic background. The activities of ceftazidime, ceftaroline, and aztreonam alone and in combination with 4mg/L of avibactam, as well as comparator agents, were assessed against a unique collection of isogenic strains of E. coli carrying selected extended-spectrum, inhibitor-resistant, and/or carbapenem-hydrolyzing bla genes. When combined with avibactam, ceftazidime, ceftaroline, or aztreonam MICs were reduced for 91.4%, 80.0%, and 80.0% of isolates, respectively. The data presented add to our understanding of the microbiologic spectrum of these β-lactams with avibactam and serve as a reference for further studies. Published by Elsevier Inc.
    Diagnostic Microbiology and Infectious Disease 02/2015; 82(1). DOI:10.1016/j.diagmicrobio.2015.02.003 · 2.57 Impact Factor
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    ABSTRACT: KPC-2 is the most prevalent class A carbapenemase in the world. Previously, KPC-2 was shown to hydrolyze the β-lactamase inhibitors clavulanic acid, sulbactam, and tazobactam. In addition, substitutions at amino acid position R220 in the KPC-2 β-lactamase also increased resistance to clavulanic acid. A novel bridged diazabicyclooctane (DBO) non-β-lactam β-lactamase inhibitor, avibactam was shown to inactivate the KPC-2 β-lactamase. To better understand the mechanistic basis for inhibition of KPC-2 by avibactam, we tested the potency of ampicillin-avibactam and ceftazidime-avibactam against engineered variants of the KPC-2 β-lactamase that possessed single amino acid substitutions at important sites (i.e., Ambler positions 69, 130, 234, 220, and 276) that were previously shown to confer inhibitor resistance in TEM and SHV β-lactamases. To this end, we performed susceptibility testing, biochemical assays, and molecular modeling. E. coli DH10B carrying KPC-2 β-lactamase variants with substitutions of S130G, K234R, and R220M demonstrated elevated MICs for only the ampicillin-avibactam combinations (e.g., 512, 64, and 32 mg/L, respectively vs. wild-type KPC-2 at 2-8 mg/L). Steady-state kinetics revealed that the S130G variant of KPC-2 resisted inactivation by avibactam; k2/K was significantly lowered 4 log values for the S130G variant compared to the wild type enzyme (21,580 M(-1)s(-1) to 1.2 M(-1)s(-1)). Molecular modeling and molecular dynamics simulations suggest that the mobility of K73 and its ability to activate S70 (i.e., function as a general base) may be impaired in the S130G variant of KPC-2, thereby explaining the slowed acylation. Moreover, we also advance that the protonation of the sulfate nitrogen of avibactam may be slowed in the S130G variant as S130 is the likely proton donor and another residue, possibly K234 must compensate. Our findings show that residues S130 as well as K234 and R220 contribute significantly to the mechanism of avibactam inactivation of KPC-2. Fortunately, the emergence of S130G, K234R, and R220M variants of KPC in the clinic should not result in failure of ceftazidime-avibactam as the ceftazidime partner is potent against E. coli DH10B strains possessing all of these variants. Copyright © 2015, American Society for Microbiology. All Rights Reserved.
    Antimicrobial Agents and Chemotherapy 02/2015; DOI:10.1128/AAC.04406-14 · 4.45 Impact Factor
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    ABSTRACT: Acinetobacter baumannii is an important cause of healthcare-associated infections, and is particularly problematic among patients who undergo organ transplantation. We describe a case of fulminant sepsis caused by carbapenem-resistant A. baumannii harboring the blaOXA-23 carbapenemase gene and belonging to international clone II. This isolate led to the death of a patient 6 days after simultaneous kidney-pancreas transplantation. Autopsy findings revealed acute mitral valve endocarditis, myocarditis, splenic and renal emboli, peritonitis, and pneumonia. This case highlights the severe nature of certain A. baumannii infections and the vulnerability of transplanted patients to the increasingly intractable “high-risk” clones of multidrug-resistant organisms.
    Transplant Infectious Disease 02/2015; 17(2). DOI:10.1111/tid.12351 · 1.98 Impact Factor
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    ABSTRACT: For the class A β-lactamase SHV-1, the kinetic and mechanistic properties of the clinically used inhibitor sulbactam are compared with the sulbactam analog substituted in its 6β position by a CH2OH group (6β-(hydroxymethyl)penicillanic acid). The 6β substitution improves both in vitro and microbiological inhibitory properties of sulbactam. Base hydrolysis of both compounds was studied by Raman and NMR spectroscopies and showed that lactam ring opening is followed by fragmentation of the dioxothiazolidine ring leading to formation of the iminium ion within 3 min. The iminium ion slowly loses a proton and converts to cis-enamine (which is a β-aminoacrylate) in 1 h for sulbactam and in 4 h for 6β-(hydroxymethyl) sulbactam. Rapid mix-rapid freeze Raman spectroscopy was used to follow the reactions between the two sulfones and SHV-1. Within 23 ms, a 10-fold excess of sulbactam was entirely hydrolyzed to give a cis-enamine product. In contrast, the 6β-(hydroxymethyl) sulbactam formed longer-lived acyl-enzyme intermediates that are a mixture of imine and enamines. Single crystal Raman studies, soaking in and washing out unreacted substrates, revealed stable populations of imine and trans-enamine acyl enzymes. The corresponding X-ray crystallographic data are consonant with the Raman data and also reveal the role played by the 6β-hydroxymethyl group in retarding hydrolysis of the acyl enzymes. The 6β-hydroxymethyl group sterically hinders approach of the water molecule as well as restraining the side chain of E166 that facilitates hydrolysis.
    Biochemistry 01/2015; 54(3):734–743. · 3.19 Impact Factor
  • Federico Perez, Robert A Bonomo
    Clinical Infectious Diseases 01/2015; DOI:10.1093/cid/civ007 · 9.42 Impact Factor

Publication Stats

10k Citations
1,525.81 Total Impact Points

Institutions

  • 2002–2015
    • Case Western Reserve University School of Medicine
      • • Department of Molecular Biology and Microbiology
      • • Department of Medicine
      Cleveland, Ohio, United States
  • 1996–2015
    • Louis Stokes Cleveland VA Medical Center
      Cleveland, Ohio, United States
  • 1992–2015
    • Case Western Reserve University
      • • Department of Molecular Biology and Microbiology
      • • School of Medicine
      • • Department of Pharmacology
      • • Department of Biochemistry
      • • Department of Chemistry
      • • Division of Infectious Diseases and HIV Medicine
      Cleveland, Ohio, United States
  • 2014
    • University of North Carolina at Chapel Hill
      North Carolina, United States
    • Cleveland Clinic
      • Department of Infectious Disease
      Cleveland, Ohio, United States
  • 2013
    • Northeast Ohio Medical University
      • Department of Internal Medicine
      Ravenna, Ohio, United States
  • 2012
    • University of British Columbia - Vancouver
      • Department of Microbiology and Immunology
      Vancouver, British Columbia, Canada
  • 2010–2012
    • Southern Methodist University
      • Department of Chemistry
      Dallas, Texas, United States
  • 1997–2012
    • Cleveland State University
      • Department of Chemistry
      Cleveland, Ohio, United States
  • 2011
    • Detroit Medical Center
      Detroit, Michigan, United States
    • Centre Hospitalier Universitaire de Clermont-Ferrand
      Clermont, Auvergne, France
  • 2009–2011
    • Mount Sinai School of Medicine
      • Department of Medicine
      Manhattan, NY, United States
    • Saint Edward's University
      Austin, Texas, United States
  • 2008–2010
    • U.S. Department of Veterans Affairs
      Washington, Washington, D.C., United States
  • 2007–2008
    • Emory University
      • Department of Microbiology and Immunology
      Atlanta, GA, United States
  • 2005
    • Semmelweis University
      Budapeŝto, Budapest, Hungary
  • 2003–2005
    • University of Pittsburgh
      • Division of Infectious Diseases
      Pittsburgh, PA, United States
  • 2004
    • Minneapolis Veterans Affairs Hospital
      Minneapolis, Minnesota, United States
  • 1998–2004
    • University of Connecticut
      • Department of Molecular and Cell Biology
      Storrs, CT, United States