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The cell-surface protein FrpC from Neisseria meningitidis has been engineered to allow covalent coupling between proteins, because it generates a reactive anhydride when exposed to calcium. [42] The bacterium also expresses unique enzymes able to cleave IgA antibodies. [43]
Capsules, made of carbohydrate, form part of the outer structure of many bacterial cells including Neisseria meningitidis. Capsules play important roles in immune evasion, as they inhibit phagocytosis, as well as protecting the bacteria while outside the host. Another group of virulence factors possessed by bacteria are immunoglobulin (Ig ...
This enzyme is secreted by Gram-negative bacteria Neisseria gonorrhoeae, Neisseria meningitidis, Haemophilus influenzae, and Gram-positive Streptococcus pneumoniae. The action of IgA protease allows the above mentioned bacteria to adhere to mucous membranes.
Neisseria is a large genus of bacteria that colonize the mucosal surfaces of many animals. Of the 11 species that colonize humans, only two are pathogens , N. meningitidis and N. gonorrhoeae . Neisseria species are Gram-negative bacteria included among the Pseudomonadota , a large group of Gram-negative forms.
MLST has provided a more richly textured picture of bacteria within human populations and on strain variants that may be pathogenic to human, plants and animals. MLST technique was first used by Maiden et al. (1) to characterize Neisseria meningitidis using six loci. The application of MLST has clearly resolved the major meningococcal lineages ...
Meningococcal disease describes infections caused by the bacterium Neisseria meningitidis (also termed meningococcus). [1] It has a high mortality rate if untreated but is vaccine-preventable. [2] While best known as a cause of meningitis, it can also result in sepsis, which is an even more damaging and dangerous condition.
However the temperature for expression of Neisseria virulence-associated traits is 42 °C while other bacterial pathogen RNATs require 37 °C. This is probably because N. meningitidis is an obligate commensal of the human nasopharynx and becomes pathogenic during inflammation due to viral infection.
The crystalline structure from Neisseria meningitidis was computed through x-ray diffraction techniques at a resolution of 2.40 Å. Pyruvate, water dikinase in Neisseria meningitidis is 794 amino acids in length and has two active sites: one at at position 422 and position 752. [3]