scholarly journals Crystal structure of aminopeptidase N from human pathogen Neisseria meningitidis

2007 ◽  
Vol 70 (1) ◽  
pp. 273-279 ◽  
Author(s):  
B. Nocek ◽  
R. Mulligan ◽  
M. Bargassa ◽  
F. Collart ◽  
A. Joachimiak
Keyword(s):  
Crystal Structure ◽  
Neisseria Meningitidis ◽  
Aminopeptidase N ◽  
Human Pathogen

scholarly journals Colonization of dermal arterioles by Neisseria meningitidis provides a safe haven from neutrophils

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Valeria Manriquez ◽  
Pierre Nivoit ◽  
Tomas Urbina ◽  
Hebert Echenique-Rivera ◽  
Keira Melican ◽  
...  
Keyword(s):  
Neisseria Meningitidis ◽  
Inflammatory Infiltrate ◽  
Immune Escape ◽  
Systemic Disease ◽  
Neutrophil Recruitment ◽  
Vascular Damage ◽  
Bacterial Burden ◽  
Human Pathogen ◽  
Humanized Mouse ◽  
Humanized Mouse Model

AbstractThe human pathogen Neisseria meningitidis can cause meningitis and fatal systemic disease. The bacteria colonize blood vessels and rapidly cause vascular damage, despite a neutrophil-rich inflammatory infiltrate. Here, we use a humanized mouse model to show that vascular colonization leads to the recruitment of neutrophils, which partially reduce bacterial burden and vascular damage. This partial effect is due to the ability of bacteria to colonize capillaries, venules and arterioles, as observed in human samples. In venules, potent neutrophil recruitment allows efficient bacterial phagocytosis. In contrast, in infected capillaries and arterioles, adhesion molecules such as E-Selectin are not expressed on the endothelium, and intravascular neutrophil recruitment is minimal. Our results indicate that the colonization of capillaries and arterioles by N. meningitidis creates an intravascular niche that precludes the action of neutrophils, resulting in immune escape and progression of the infection.

Crystal structure of truncated FlgD from the human pathogen Helicobacter pylori

2016 ◽  
Vol 194 (2) ◽  
pp. 147-155 ◽  
Author(s):  
Ivana Pulić ◽  
Laura Cendron ◽  
Marco Salamina ◽  
Patrizia Polverino de Laureto ◽  
Dubravka Matković-Čalogović ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Helicobacter Pylori ◽  
Human Pathogen

scholarly journals Structure of the regulatory domain of the LysR family regulator NMB2055 (MetR-like protein) fromNeisseria meningitidis

2012 ◽  
Vol 68 (7) ◽  
pp. 730-737 ◽  
Author(s):  
Sarah Sainsbury ◽  
Jingshan Ren ◽  
Nigel J. Saunders ◽  
David I. Stuart ◽  
Raymond J. Owens
Keyword(s):  
Crystal Structure ◽  
Transcription Factors ◽  
Neisseria Meningitidis ◽  
Disulfide Bond ◽  
Binding Pocket ◽  
Cysteine Residues ◽  
Regulatory Domain ◽  
High Degree ◽  
Effector Binding ◽  
Lysr Family

The crystal structure of the regulatory domain of NMB2055, a putative MetR regulator fromNeisseria meningitidis, is reported at 2.5 Å resolution. The structure revealed that there is a disulfide bond inside the predicted effector-binding pocket of the regulatory domain. Mutation of the cysteines (Cys103 and Cys106) that form the disulfide bond to serines resulted in significant changes to the structure of the effector pocket. Taken together with the high degree of conservation of these cysteine residues within MetR-related transcription factors, it is suggested that the Cys103 and Cys106 residues play an important role in the function of MetR regulators.

scholarly journals NeMeSys: a biological resource for narrowing the gap between sequence and function in the human pathogen Neisseria meningitidis

2009 ◽  
Vol 10 (10) ◽  
pp. R110 ◽  
Author(s):  
Christophe Rusniok ◽  
David Vallenet ◽  
Stéphanie Floquet ◽  
Helen Ewles ◽  
Coralie Mouzé-Soulama ◽  
...  
Keyword(s):  
Neisseria Meningitidis ◽  
Human Pathogen ◽  
Biological Resource ◽  
And Function

scholarly journals Identification and Characterization of Genes Required for Competence in Neisseria meningitidis

2005 ◽  
Vol 187 (9) ◽  
pp. 3273-3276 ◽  
Author(s):  
Yao-Hui Sun ◽  
Rachel Exley ◽  
Yanwen Li ◽  
David Goulding ◽  
Christoph Tang
Keyword(s):  
Neisseria Meningitidis ◽  
Human Pathogen ◽  
Transposon Insertions ◽  
Identification And Characterization

ABSTRACT We have identified genes required for competence of Neisseria meningitidis, a naturally transformable human pathogen. Although not comprehensive, our analysis identified competence-defective mutants with transposon insertions in genes not previously implicated in this process in Neisseria.

scholarly journals Characterization of a transcriptional TPP riboswitch in the human pathogen Neisseria meningitidis

RNA Biology ◽  
2020 ◽  
Vol 17 (5) ◽  
pp. 718-730
Author(s):  
Francesco Righetti ◽  
Solange Lise Materne ◽  
John Boss ◽  
Hannes Eichner ◽  
Emmanuelle Charpentier ◽  
...  
Keyword(s):  
Neisseria Meningitidis ◽  
Human Pathogen

scholarly journals A generic mechanism in Neisseria meningitidis for enhanced resistance against bactericidal antibodies

2008 ◽  
Vol 205 (6) ◽  
pp. 1423-1434 ◽  
Author(s):  
Maria Jose Uria ◽  
Qian Zhang ◽  
Yanwen Li ◽  
Angel Chan ◽  
Rachel M. Exley ◽  
...  
Keyword(s):  
Neisseria Meningitidis ◽  
Insertion Sequence ◽  
Alternative Pathway ◽  
Polysialic Acid ◽  
Systemic Infection ◽  
Human Pathogen ◽  
Transcript Levels ◽  
Whole Cells ◽  
Enhanced Resistance ◽  
Alternative Pathway Of Complement

The presence of serum bactericidal antibodies is a proven correlate of protection against systemic infection with the important human pathogen Neisseria meningitidis. We have identified three serogroup C N. meningitidis (MenC) isolates recovered from patients with invasive meningococcal disease that resist killing by bactericidal antibodies induced by the MenC conjugate vaccine. None of the patients had received the vaccine, which has been successfully introduced in countries in North America and Europe. The increased resistance was not caused by changes either in lipopolysaccharide sialylation or acetylation of the α2-9–linked polysialic acid capsule. Instead, the resistance of the isolates resulted from the presence of an insertion sequence, IS1301, in the intergenic region (IGR) between the sia and ctr operons, which are necessary for capsule biosynthesis and export, respectively. The insertion sequence led to an increase in the transcript levels of surrounding genes and the amount of capsule expressed by the strains. The increased amount of capsule was associated with down-regulation of the alternative pathway of complement activation, providing a generic mechanism by which the bacterium protects itself against bactericidal antibodies. The strains with IS1301 in the IGR avoided complement-mediated lysis in the presence of bactericidal antibodies directed at the outer membrane protein, PorA, or raised against whole cells.

Neisseria meningitidis

1985 ◽  
Vol 6 (1) ◽  
pp. 37-40 ◽  
Author(s):  
David S. Stephens
Keyword(s):  
Neisseria Meningitidis ◽  
Spinal Fluid ◽  
Human Pathogen ◽  
Fatal Sepsis

Neisseria meningitidisis an exclusive human pathogen. The organism was first recognized by Weichselbaum in 1887 in the spinal fluid of six patients with acute cerebrospinal meningitis. He called itDiplococcus intracellularis meningitidisbecause of the presence of the organism within leukocytes from the spinal fluid. Subsequent studies established the meningococcus as the cause of epidemic cerebrospinal fever and placed the organism in the genusNeisseria. Despite the availability of effective antimicrobials and partially effective vaccines,N. meningitidisremains one of the most frequent causes of rapidly fatal sepsis and meningitis.

scholarly journals Crystal Structure of Outer Membrane Protein NMB0315 from Neisseria meningitidis

PLoS ONE ◽  
2011 ◽  
Vol 6 (10) ◽  
pp. e26845 ◽  
Author(s):  
Xiangyu Wang ◽  
Xue Yang ◽  
Chunting Yang ◽  
Zhenhua Wu ◽  
Honglin Xu ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Membrane Protein ◽  
Neisseria Meningitidis ◽  
Outer Membrane ◽  
Outer Membrane Protein
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