Am J Infect Control 2007, 35:86–88.PubMedCrossRef 27. Gillor O, Etzion A, Riley MA: The dual role of bacteriocins as anti- and probiotics. Appl Microbiol Biotechnol 2008, 81:591–606.PubMedCrossRef Competing interests The authors declare that they have no competing interests. Authors’ contributions CK carried out all phenotypic work, DNA extraction, PCR, sequencing, and drafted the manuscript. RG conceived selleckchem of the study and participated

in its design, and edited the manuscript. LCS had done the analysis of the sequencing data. AS have designed the study. VK monitored the mother and the neonates for Selleckchem HDAC inhibitor clinical outcomes and have trained the field workers. SA supervised the monitoring of the clinical outcomes. HC designed the clinical study and edited the manuscript. SS and MD had done the final editing and approved the final manuscript. All authors have read and approved the final manuscript.”
“Background H. influenzae is a fastidious, Gram-negative, opportunistic pathogen that belongs to the family Pasteurellaceae and is a common commensal in the nasopharynx of humans [1, 2]. H. influenzae is a causative

agent of both invasive and non-invasive diseases including bacteremia, meningitis, respiratory infections, and otitis media [1]. Invasive disease may be caused by either encapsulated or nonencapsulated strains [3], whereas non-invasive diseases are primarily caused by nonencapsulated, nontypeable H. influenzae[4]. Like most other bacteria, H. influenzae requires iron for growth but it also has an absolute requirement PD184352 (CI-1040) for a porphyrin source, in the form of protoporphyrin

IX (PPIX) or heme, to grow aerobically [5]. This PARP inhibitor drugs requirement for a porphyrin source is due to the lack of enzymes required to synthesize the protoporphyrin ring. Therefore, H. influenzae must acquire heme from host sources in order to establish and sustain an infection [6]. Potential sources of heme in the human host are limited; heme is generally intracellular, bound by hemoglobin or other heme-containing proteins, and there is no significant source of PPIX [7, 8]. H. influenzae has evolved multiple mechanisms to counter and exploit host mechanisms for sequestering heme from invading pathogens [9]. Although many of these mechanisms are transcriptionally upregulated in response to iron and heme restriction, the specific regulation of many of these systems is largely uncharacterized in H. influenzae[10, 11]. The RNA-binding protein Hfq is an important regulator of gene transcription, including the transcription of iron responsive genes, in many bacterial pathogens such as Escherichia coli, Neisseria meningitidis, and Salmonella enterica[12–14]. The Hfq protein was originally described as a host factor required for the synthesis of bacteriophage Qβ RNA in E. coli and belongs to the Sm and Sm-like family of proteins that are found in both prokaryotes and eukaryotes [15, 16].