Looking for breakthrough ideas for innovation challenges? Try Patsnap Eureka!

Complement factor h-based assays for serum bactericidal activity against neisseria meningitidis

A Neisseria and bactericidal technology, which is applied in the field of identification of the bactericidal activity of Neisseria meningitidis serum based on complement factor H, and can solve problems such as the actual mechanism of vaccine-induced antibody protection that cannot be accurately or completely reflected.

Inactive Publication Date: 2011-09-28
CHILDREN S HOSPITAL &RES CENT AT OAKLAN +2
View PDF5 Cites 5 Cited by
  • Summary
  • Abstract
  • Description
  • Claims
  • Application Information

AI Technical Summary

Problems solved by technology

[0009] Therefore, the correlations observed with rabbit complement may not accurately or completely reflect the actual mechanism of protection conferred by vaccine-induced antibodies

Method used

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
View more

Image

Smart Image Click on the blue labels to locate them in the text.
Viewing Examples
Smart Image
  • Complement factor h-based assays for serum bactericidal activity against neisseria meningitidis
  • Complement factor h-based assays for serum bactericidal activity against neisseria meningitidis
  • Complement factor h-based assays for serum bactericidal activity against neisseria meningitidis

Examples

Experimental program
Comparison scheme
Effect test

Embodiment 1

[0153] Example 1: Species specificity of binding of primate fH to N. meningitidis

[0154] Polyclonal anti-human fH recognizes fH in heat-inactivated sera from humans as well as non-human primates ( figure 1 A, Lane labeled ("serum only")), thus can be used to test the binding of primate fH to bacteria. Binding of fH to strain H44 / 76 in primate heat-inactivated serum is shown in the lane labeled "serum + bacteria". Heat treatment does not affect the binding properties of fH (Jarva, H. et al. (2002) J Immunol 168:1886-1894; Ram, S. et al. (1998) J Exp Med 188:671-680). Bacteria incubated with human serum (positive control) showed the greatest fH binding, whereas fH binding was at low levels in chimpanzee serum and undetectable in baboon and rhesus monkey sera.

Embodiment 2

[0155] Example 2: Rat or rabbit fH does not compete with human fH for binding to Neisseria meningitidis

[0156] Indirect flow cytometric assays were used to determine whether heat-inactivated rat or rabbit fH (in their respective heat-inactivated sera) competed with biotinylated human fH for binding to the same ligand on live N. meningitidis. Addition of 40% heat-inactivated rat or rabbit serum (highest concentration tested) did not inhibit binding of biotinylated human fH to N. meningitidis, whereas addition of 40% heat-inactivated human serum as a positive control did Binding of biotinylated human fH ( figure 1 B and 1C). These data indicate that rat and rabbit fH bind different ligands on N. meningitidis than human fH. Although the possibility that the binding sites of rat and rabbit fH on meningococci differ from that of human fH cannot be ruled out, an amino acid sequence alignment of human fH, macaque fH, and rat fH (from the NCBI database) shows that , human and ma...

Embodiment 3

[0157] Example 3: Effect of Human fH Added to Juvenile Rat Serum on Neisseria meningitidis Survival

[0158] The effect of adding human fH to the sera of young rats was determined on the survival of three strains of N. meningitidis in a mixture incubated at 37°C for 1 hour ( figure 2 ). Each serum was tested at concentrations of 20%, 40% and 60%. When no fH was added, compared with their respective zero-time survival rates, the two strains NZ98 / 254 and Cu385 (respectively figure 2 The survival rate increased by more than 150% during the incubation period. In contrast, the third strain H44 / 76 survived at all three serum concentrations ( figure 2 lower graph) were reduced by 40% -60%. When human fH was added to the reaction at a concentration of 50 μg / ml, the corresponding survival rate of strain H44 / 76 was increased by >150% (e.g., 60% serum containing human fH compared to 26% survival without human fH The survival rate in was 152%, P<0.001). The survival of one of the...

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

PUM

No PUM Login to View More

Abstract

Assays for detection of bactericidal anti-Neisserial antibodies using a factor H polypeptide having a human amino acid sequence that mediates binding to Neisserial factor H binding protein (fhBp) are provided, as well as non-human animal models of Neisserial infection.

Description

[0001] Statement Regarding Federally Funded Research [0002] This study was supported by grants RO1 AI46464 and RO1 AI054544 from the Public Health Service of the National Institute of Allergy and Infectious Diseases. Research at the Children's Hospital Oakland Research Institute was supported by grant number CO6RR-16226 from the National Center for Research Resources (NIH) Research Facilities Improvement Program equipment. The Federal Government has certain rights in this invention. technical field [0003] The present invention relates to the identification of the bactericidal activity of antibodies against Neisseria meningitidis. Background technique [0004] Neisseria meningitidis is a commensal organism commonly found in the throat of healthy adolescents (Maiden, M.C. et al. (2008) J Infect Dis.; Mueller, J.E. et al. (2007) Emerg Infect Dis 13:847-854; Trotter , C.L. et al. (2006) Epidemiol Infect 134:556-566; Bogaert, D. et al. (2005) Clin Infect Dis 40:899-902; V...

Claims

the structure of the environmentally friendly knitted fabric provided by the present invention; figure 2 Flow chart of the yarn wrapping machine for environmentally friendly knitted fabrics and storage devices; image 3 Is the parameter map of the yarn covering machine
Login to View More

Application Information

Patent Timeline
no application Login to View More
IPC IPC(8): C12Q1/02A01K67/027
CPCG01N2469/20G01N2333/22G01N33/6857G01N2333/4716
Inventor D·M·格拉诺夫J·A·韦尔施尔S·拉姆
Owner CHILDREN S HOSPITAL &RES CENT AT OAKLAN
Who we serve
  • R&D Engineer
  • R&D Manager
  • IP Professional
Why Patsnap Eureka
  • Industry Leading Data Capabilities
  • Powerful AI technology
  • Patent DNA Extraction
Social media
Patsnap Eureka Blog
Learn More
PatSnap group products

Browse by: Latest US Patents, China's latest patents, Technical Efficacy Thesaurus, Application Domain, Technology Topic, Popular Technical Reports.

© 2024 PatSnap. All rights reserved.Legal|Privacy policy|Modern Slavery Act Transparency Statement|Sitemap|About US| Contact US: help@patsnap.com