Functional analysis of Bacillus anthracis protective antigen by using neutralizing monoclonal antibodies.
about
Human monoclonal antibodies against anthrax lethal factor and protective antigen act independently to protect against Bacillus anthracis infection and enhance endogenous immunity to anthraxMonoclonal Antibody Combinations that Present Synergistic Neutralizing Activity: A Platform for Next-Generation Anti-Toxin DrugsCrystal Structure of the Engineered Neutralizing Antibody M18 Complexed to Domain 4 of the Anthrax Protective AntigenIn vitro and in vivo characterization of anthrax anti-protective antigen and anti-lethal factor monoclonal antibodies after passive transfer in a mouse lethal toxin challenge model to define correlates of immunityIsolation and chimerization of a highly neutralizing antibody conferring passive protection against lethal Bacillus anthracis infectionMonoclonal antibody therapies against anthraxHigh-affinity, human antibody-like antibody fragment (single-chain variable fragment) neutralizing the lethal factor (LF) of Bacillus anthracis by inhibiting protective antigen-LF complex formation.Selection and characterization of human antibodies neutralizing Bacillus anthracis toxin.Immunogenicity of Bacillus anthracis protective antigen domains and efficacy of elicited antibody responses depend on host genetic background.Neutralizing monoclonal antibodies directed against defined linear epitopes on domain 4 of anthrax protective antigenNeutralizing monoclonal antibody to edema toxin and its effect on murine anthrax.Select human anthrax protective antigen epitope-specific antibodies provide protection from lethal toxin challenge.An anthrax lethal factor-neutralizing monoclonal antibody protects rats before and after challenge with anthrax toxin.Anthrax toxin-neutralizing antibody reconfigures the protective antigen heptamer into a supercomplex.Preparation and evaluation of human-murine chimeric antibody against protective antigen of Bacillus anthracis.A monoclonal antibody to Bacillus anthracis protective antigen defines a neutralizing epitope in domain 1Mapping the epitopes of a neutralizing antibody fragment directed against the lethal factor of Bacillus anthracis and cross-reacting with the homologous edema factorProphylaxis and therapy of inhalational anthrax by a novel monoclonal antibody to protective antigen that mimics vaccine-induced immunity.Anthrax vaccination induced anti-lethal factor IgG: fine specificity and neutralizing capacity.Antibodies against anthrax: mechanisms of action and clinical applications.Functional analysis of neutralizing antibodies against Clostridium perfringens epsilon-toxinAnalysis of epitope information related to Bacillus anthracis and Clostridium botulinum.Analysis of defined combinations of monoclonal antibodies in anthrax toxin neutralization assays and their synergistic action.Monoclonal antibodies and toxins--a perspective on function and isotype.Rapid generation of an anthrax immunotherapeutic from goats using a novel non-toxic muramyl dipeptide adjuvant.Selection and evaluation of the immunogenicity of protective antigen mutants as anthrax vaccine candidates.MHC class II and non-MHC class II genes differentially influence humoral immunity to Bacillus anthracis lethal factor and protective antigen.Serum IgG antibody response to the protective antigen (PA) of Bacillus anthracis induced by anthrax vaccine adsorbed (AVA) among U.S. military personnel.Sortase-conjugation generates a capsule vaccine that protects guinea pigs against Bacillus anthracisPast, imminent and future human medical countermeasures for anthrax.Enhancement of antibody responses to Bacillus anthracis protective antigen domain IV by use of calreticulin as a chimeric molecular adjuvantRecombinant vaccine displaying the loop-neutralizing determinant from protective antigen completely protects rabbits from experimental inhalation anthraxDisease-enhancing antibodies improve the efficacy of bacterial toxin-neutralizing antibodiesCombinations of monoclonal antibodies to anthrax toxin manifest new properties in neutralization assays.Effective delivery of antisense peptide nucleic acid oligomers into cells by anthrax protective antigenSequential B-cell epitopes of Bacillus anthracis lethal factor bind lethal toxin-neutralizing antibodiesAnti-toxin antibodies in prophylaxis and treatment of inhalation anthrax.Synthetic peptide vaccine targeting a cryptic neutralizing epitope in domain 2 of Bacillus anthracis protective antigen.Novel chimpanzee/human monoclonal antibodies that neutralize anthrax lethal factor, and evidence for possible synergy with anti-protective antigen antibody.Identification of linear epitopes in Bacillus anthracis protective antigen bound by neutralizing antibodies.
P2860
Q24682011-88AA3389-AC09-4A38-BD96-2BC65B30CD36Q26863621-A67BB52A-13A4-456A-8881-5EE032DD5C12Q27654632-C389C49B-7D18-434C-A871-0DF624B90D88Q28383065-9D940BF2-EBDE-497F-8D69-0B9274061994Q28389813-1C9AB692-8B13-4CE5-9703-2C702AE56A52Q28393072-629B50EE-C3B8-458A-B787-6ED0C0F5161EQ33285349-4B99507E-BFFC-441D-98F0-D659613C3BD7Q33306246-C56DB5C8-DCC9-4008-8D97-75091EFE603FQ33334776-2A4D9D0A-6DC5-4C66-8B20-EB1082801B48Q33496407-C7505DDC-5668-4CE7-9012-2505F116F32FQ33877222-B713EF69-D09F-4BF5-BFBC-DEB5FC416DD4Q33936452-911C9B0C-BEAD-43C9-AB7D-872674FC7BD3Q34033505-541F36BF-8EE4-4D4C-9683-06FCA2B101FFQ34069693-4D50BF62-AE4C-4678-9A93-D68BCA3D3CE0Q34486875-77FD2316-04A4-43DE-89E5-2171895156CEQ34721109-B8A3F13D-24E6-4576-878F-45F7EEAB5570Q34761514-A372D608-9F25-43B0-9A05-D548AB5E373EQ35073821-83F9A5FA-462E-4C54-A6E2-D554D358F15EQ35599606-D5BC8257-E796-435D-994D-3D5C512F78EEQ35610439-E93F96F4-866D-47CD-84D9-F92D4FF21A17Q35783925-260605BE-D7B0-42A3-9ABE-D7A13F0F25DEQ35869311-9075A6C0-7538-4A04-BBB5-F83AB4AB42C9Q35940722-6BE250CB-251A-4829-AB57-E9423CECCD46Q36099489-4C15EF0D-B0A5-4061-AF32-D68D500CC1E4Q36183762-78AC06B0-6FA7-4688-8DF4-8C217C736608Q36478354-E144A218-925E-43C3-8B2E-A60EBA3A8E79Q36482706-174AA78F-F6B0-47CD-B1DD-6CBDFF9A6C74Q36496954-94C3A6BD-639F-426A-B47D-D99801D9301BQ36513949-A6EEDFCC-DA81-4490-A5BD-D0778D862A6AQ36565152-1E0D9044-1160-4A7C-9B51-B1D4BB0777A9Q36593900-DE9F1FF4-A78F-470C-A438-B459522448C6Q36668524-C1FBF6E9-9369-4FB8-90BB-AEE009B02BB0Q36786293-1770E240-F765-4BAE-BC35-D70FB4F01995Q36911369-7C44D461-FED9-4F0F-A6B3-7ACD5AFFB983Q36968203-DC060C92-285A-4C14-9DB8-56A46915A0C2Q37033046-391D546C-514D-49A8-A61E-528A13AF7271Q37262118-FB04E025-BDAA-40A2-A359-761D01EB1837Q37274918-220BAE3C-FEB8-4F5C-BD74-DFB9B980A245Q37333457-CC54AE1F-431A-4BDD-8F77-A0B25B8C68E4Q37375729-A822CE72-E12C-4422-ACF4-3F18185A076C
P2860
Functional analysis of Bacillus anthracis protective antigen by using neutralizing monoclonal antibodies.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
@zh
2004年论文
@zh-cn
name
Functional analysis of Bacillu ...... alizing monoclonal antibodies.
@en
type
label
Functional analysis of Bacillu ...... alizing monoclonal antibodies.
@en
prefLabel
Functional analysis of Bacillu ...... alizing monoclonal antibodies.
@en
P2093
P2860
P1476
Functional analysis of Bacillu ...... alizing monoclonal antibodies.
@en
P2093
Annie Landier
Fabien Brossier
Martine Lévy
Michèle Mock
Pierre Lafaye
P2860
P304
P356
10.1128/IAI.72.11.6313-6317.2004
P407
P577
2004-11-01T00:00:00Z