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  • 1
    Language: English
    In: BBA - Biomembranes, November 2015, Vol.1848(11), pp.3026-3031
    Description: Antimicrobial peptides (AMPs) play an important role as a host defense against microbial pathogens and are key components of the human innate immune response. frequently colonizes the human nasopharynx as a commensal but also is a worldwide cause of epidemic meningitis and rapidly fatal sepsis. In the human respiratory tract, the only known reservoir of , meningococci are exposed to human endogenous AMPs. Thus, it is not surprising that meningococci have evolved effective mechanisms to confer intrinsic and high levels of resistance to the action of AMPs. This article reviews the current knowledge about AMP resistance mechanisms employed by . Two major resistance mechanisms employed by meningococci are the constitutive modification of the lipid A head groups of lipooligosaccharides by phosphoethanolamine and the active efflux pump mediated excretion of AMPs. Other factors influencing AMP resistance, such as the major porin PorB, the pilin biogenesis apparatus, and capsular polysaccharides, have also been identified. Even with an inherently high intrinsic resistance, several AMP resistance determinants can be further induced upon exposure to AMPs. Many well-characterized AMP resistance mechanisms in other Gram-negative bacteria are not found in meningococci. Thus, utilizes a limited but highly effective set of molecular mechanisms to mediate antimicrobial peptide resistance. This article is part of a Special Issue entitled: Bacterial Resistance to Antimicrobial Peptides.
    Keywords: Neisseria Meningitidis ; Antimicrobial Resistance ; Efflux Pump ; Phosphoethanolamine Modification of Lipid A ; Chemistry
    ISSN: 0005-2736
    E-ISSN: 1879-2642
    E-ISSN: 18782434
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  • 2
    Language: English
    In: The Lancet, 18 February 2012, Vol.379(9816), pp.592-594
    Description: In The Lancet, María Elena Santolaya and colleagues1 describe the immunogenicity and safety in healthy Hispanic adolescents of a new multicomponent vaccine, 4CMenB, a potential breakthrough in protection against meningitis, sepsis, and other infections caused by Neisseria meningitidis serogroup B. With the successful development and use of eff ective polysaccharideprotein glycoconjugate vaccines for serogroups A, C, Y, and W-135,2,3 serogroup B N meningitidis (distinguished by the expression of an [α2[arrow right]8]-linked polysialic acid capsule) is now the leading cause of meningococcal disease, especially in infants and young children in many countries.4,5 No vaccines are in routine use for the prevention of serogroup B meningococcal disease. Because the serogroup B polysaccharide resembles the human neural cell adhesion molecule, which results in poor immunogenicity, it has not been developed as a vaccine candidate.
    Keywords: Medicine
    ISSN: 0140-6736
    E-ISSN: 1474-547X
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  • 3
    Language: English
    In: Biochemical and Biophysical Research Communications, 10 June 2011, Vol.409(3), pp.526-531
    Description: ► Two intramolecular isopeptide bonds are present in PitB of . ► Intramolecular isopeptide bonds are not required for proteolytic stability of PitB. ► Intramolecular isopeptide bonds confer thermal stability to PitB. type 2 pili are recently identified fimbrial structures extending from the bacterial surface and formed by polymers of the structural protein PitB. Intramolecular isopeptide bonds are a characteristic of the related pilus backbone protein Spy0128 of group A streptococci. Based on the identification of conserved residues in PitB, we predicted two intramolecular isopeptide bonds in PitB. Using a combination of tandem mass spectrometry and Edman sequencing, we show that these bonds were formed between Lys -Asn and Lys -Asn in PitB. Mutant proteins lacking the intramolecular isopeptide bonds retained the proteolytic stability observed with the wild type protein. However, absence of these bonds substantially decreased the melting temperature of the PitB-derivatives, indicating a stabilizing function of these bonds in PitB of the pneumococcal type 2 pilus.
    Keywords: Fimbrial Protein ; Intramolecular Cross-Link ; Proteolytic Stability ; Thermal Stability ; Mass Spectrometry ; Biology ; Chemistry ; Anatomy & Physiology
    ISSN: 0006-291X
    E-ISSN: 1090-2104
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  • 4
    Language: English
    In: The Lancet, Feb 18, 2012, Vol.379(9816), p.592(3)
    Description: To link to full-text access for this article, visit this link: http://dx.doi.org/10.1016/S0140-6736(11)61934-X Byline: David S Stephens (a)(b) Author Affiliation: (a) Emory University School of Medicine, Atlanta, GA 30322, USA (b) VA Medical Center, Atlanta, GA 30033, USA
    Keywords: Meningitis – Prevention
    ISSN: 0140-6736
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  • 5
    Language: English
    In: Emerging Infectious Diseases, 01 June 2010, Vol.16(6), pp.955-962
    Description: To define the prevalence of pilus islet 2 (PI-2)–encoded pili in Streptococcus pneumoniae in a geographically defined area, we examined 590 S. pneumoniae isolates from population-based surveillance of invasive pneumococcal disease in Atlanta, Georgia, USA, 1994–2006. In 2006, PI-2 was present in 21% of all invasive isolates, including serotypes 1 (100%), 7F (89%), 11A (21%), 19A (40%), and 19F (75%). Only serotype 19F is included in the 7-valent pneumococcal conjugate vaccine that is in use worldwide. In 1999, PI-2-containing isolates were of the same serotypes but accounted for only 3.6% of all invasive isolates. The increase of PI-2 in 2006 resulted predominantly from the emergence of serotype 19A isolates of sequence type 320 and the expansion of serotype 7F isolates. The increase in PI-2-containing isolates and the finding that isolates of all identified serotypes expressed highly conserved PI-2 pili supports their potential as a vaccine candidate.
    Keywords: Streptococcus Pneumoniae ; Pili ; Streptococci ; Serotypes ; Bacteria ; Vaccine ; Public Health
    ISSN: 1080-6040
    E-ISSN: 1080-6059
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  • 6
    Language: English
    In: PLoS ONE, 2011, Vol.6(9), p.e25124
    Description: Streptococcus oralis, Streptococcus mitis, and Streptococcus sanguinis are members of the Mitis group of streptococci and agents of oral biofilm, dental plaque and infective endocarditis, disease processes that involve bacteria-bacteria and bacteria-host interactions. Their close relative, the human pathogen S. pneumoniae uses pilus-islet 2 (PI-2)-encoded pili to facilitate adhesion to eukaryotic cells. ; PI-2 pilus-encoding genetic islets were identified in S. oralis, S. mitis, and S. sanguinis, but were absent from other isolates of these species. The PI-2 islets resembled the genetic organization of the PI-2 islet of S. pneumoniae, but differed in the genes encoding the structural pilus proteins PitA and PitB. Two and three variants of pitA (a pseudogene in S. pneumoniae) and pitB, respectively, were identified that showed ≈20% difference in nucleotide as well as corresponding protein sequence. Species-independent combinations of pitA and pitB variants indicated prior intra- and interspecies horizontal gene transfer events. Polyclonal antisera developed against PitA and PitB of S. oralis type strain ATCC35037 revealed that PI-2 pili in oral streptococci were composed of PitA and PitB. Electronmicrographs showed pilus structures radiating 〉700 nm from the bacterial surface in the wild type strain, but not in an isogenic PI-2 deletion mutant. Anti-PitB-antiserum only reacted with pili containing the same PitB variant, whereas anti-PitA antiserum was cross-reactive with the other PitA variant. Electronic multilocus sequence analysis revealed that all PI-2-encoding oral streptococci were closely-related and cluster with non-PI-2-encoding S. oralis strains. ; This is the first identification of PI-2 pili in Mitis group oral streptococci. The findings provide a striking example of intra- and interspecies horizontal gene transfer. The PI-2 pilus diversity provides a possible key to link strain-specific bacterial interactions and/or tissue tropisms with pathogenic traits in the Mitis group streptococci.
    Keywords: Research Article ; Biology ; Medicine ; Infectious Diseases ; Microbiology ; Biochemistry
    E-ISSN: 1932-6203
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  • 7
    Language: English
    In: The Journal of infectious diseases, 01 March 2008, Vol.197(5), pp.643-5
    Keywords: Immunity, Herd -- Immunology ; Immunity, Innate -- Immunology ; Meningococcal Vaccines -- Immunology
    ISSN: 0022-1899
    E-ISSN: 15376613
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  • 8
    Language: English
    In: The Lancet Infectious Diseases, January 2017, Vol.17(1), pp.4-6
    Description: Two new meningococcal vaccines are licensed for prevention of serogroup B meningococcal disease: 4CMenB (Bexsero, Novartis, Siena, Italy) is licensed in 35 countries including the USA, Europe, Canada, and Australia, and bivalent rLP2086 (Trumenba; Pfizer, Philadelphia, PA, USA)--a bivalent factor H binding...
    Keywords: Medicine ; Public Health
    ISSN: 1473-3099
    E-ISSN: 1474-4457
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  • 9
    Language: English
    In: The Lancet Infectious Diseases, 2011, Vol.11(6), pp.421-422
    Keywords: Medicine ; Public Health
    ISSN: 1473-3099
    E-ISSN: 1474-4457
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  • 10
    Language: English
    In: Proceedings of the National Academy of Sciences of the United States, April 18, 2017, Vol.114(16), p.4237(6)
    Description: Neisseria meningitidis (Nm) clonal complex 11 (cc11) lineage is a hypervirulent pathogen responsible for outbreaks of invasive meningococcal disease, including among men who have sex with men, and is increasingly associated with urogenital infections. Recently, clusters of Nm urethritis have emerged primarily among heterosexual males in the United States. We determined that nonencapsulated meningococcal isolates from an ongoing Nm urethritis outbreak among epidemiologically unrelated men in Columbus, Ohio, are linked to increased Nm urethritis cases in multiple US cities, including Atlanta and Indianapolis, and that they form a unique clade (the US Nm urethritis clade, US_NmUC). The isolates belonged to the cc11 lineage 11.2/ET-15 with fine type of PorA P1.5-1, 10-8; FetA F3-6; PorB 2-2 and express a unique FHbp allele. A common molecular fingerprint of US_NmUC isolates was an IS1301 element in the intergenic region separating the capsule ctr-css operons and adjacent deletion of cssA/B/C and a part of csc, encoding the serogroup C capsule polymerase. This resulted in the loss of encapsulation and intrinsic lipooligosaccharide sialylation that may promote adherence to mucosal surfaces. Furthermore, we detected an IS1301-mediated inversion of an ∼20-kb sequence near the cps locus. Surprisingly, these isolates had acquired by gene conversion the complete gonococcal denitrification norB-aniA gene cassette, and strains grow well anaerobically. The cc11 US_NmUC isolates causing urethritis clusters in the United States may have adapted to a urogenital environment by loss of capsule and gene conversion of the Neisseria gonorrheae norB-aniA cassette promoting anaerobic growth.
    Keywords: Neisseria Meningitidis – Genetic Aspects ; Neisseria Meningitidis – Health Aspects
    ISSN: 0027-8424
    E-ISSN: 10916490
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