Abstract:
:The unpredictable nature of bioterrorism and the absence of real-time detection systems have highlighted the need for an efficient postexposure therapy for Bacillus anthracis infection. One approach is passive immunization through the administration of antibodies that mitigate the biological action of anthrax toxin. We isolated and characterized two protective fully human monoclonal antibodies with specificity for protective antigen (PA) and lethal factor (LF). These antibodies, designated IQNPA (anti-PA) and IQNLF (anti-LF), were developed as hybridomas from individuals immunized with licensed anthrax vaccine. The effective concentration of IQNPA that neutralized 50% of the toxin in anthrax toxin neutralization assays was 0.3 nM, while 0.1 nM IQNLF neutralized the same amount of toxin. When combined, the antibodies had additive neutralization efficacy. IQNPA binds to domain IV of PA containing the host cell receptor binding site, while IQNLF recognizes domain I containing the PA binding region in LF. A single 180-mug dose of either antibody given to A/J mice 2.5 h before challenge conferred 100% protection against a lethal intraperitoneal spore challenge with 24 50% lethal doses [LD50s] of B. anthracis Sterne and against rechallenge on day 20 with a more aggressive challenge dose of 41 LD50s. Mice treated with either antibody and infected with B. anthracis Sterne developed detectable murine anti-PA and anti-LF immunoglobulin G antibody responses by day 17 that were dependent on which antibody the mice had received. Based on these results, IQNPA and IQNLF act independently during prophylactic anthrax treatment and do not interfere with the establishment of endogenous immunity.
journal_name
Infect Immunjournal_title
Infection and immunityauthors
Albrecht MT,Li H,Williamson ED,LeButt CS,Flick-Smith HC,Quinn CP,Westra H,Galloway D,Mateczun A,Goldman S,Groen H,Baillie LWdoi
10.1128/IAI.00261-07subject
Has Abstractpub_date
2007-11-01 00:00:00pages
5425-33issue
11eissn
0019-9567issn
1098-5522pii
IAI.00261-07journal_volume
75pub_type
杂志文章abstract::An LT-B-ST (LT-B/ST) fusion peptide was constructed by genetically joining the 5' terminus of a synthetic gene coding for the heat-stable enterotoxin (ST) of Escherichia coli to the 3' terminus of the gene coding for the binding subunit of the heat-labile enterotoxin (LT-B) of E. coli. An eight-amino-acid, proline-con...
journal_title:Infection and immunity
pub_type: 杂志文章
doi:10.1128/IAI.61.11.4629-4636.1993
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journal_title:Infection and immunity
pub_type: 杂志文章
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journal_title:Infection and immunity
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journal_title:Infection and immunity
pub_type: 杂志文章
doi:10.1128/IAI.2.5.686-688.1970
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journal_title:Infection and immunity
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journal_title:Infection and immunity
pub_type: 杂志文章
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doi:10.1128/IAI.56.5.1382-1384.1988
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journal_title:Infection and immunity
pub_type: 杂志文章
doi:10.1128/IAI.55.9.2017-2020.1987
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journal_title:Infection and immunity
pub_type: 杂志文章
doi:10.1128/IAI.14.3.671-679.1976
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journal_title:Infection and immunity
pub_type: 杂志文章
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journal_title:Infection and immunity
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doi:10.1128/iai.71.1.226-233.2003
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journal_title:Infection and immunity
pub_type: 杂志文章
doi:10.1128/IAI.57.8.2301-2305.1989
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journal_title:Infection and immunity
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journal_title:Infection and immunity
pub_type: 杂志文章
doi:10.1128/IAI.54.2.435-443.1986
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journal_title:Infection and immunity
pub_type: 杂志文章
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journal_title:Infection and immunity
pub_type: 杂志文章
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journal_title:Infection and immunity
pub_type: 杂志文章
doi:10.1128/IAI.13.3.959-966.1976
更新日期:1976-03-01 00:00:00
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journal_title:Infection and immunity
pub_type: 杂志文章
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journal_title:Infection and immunity
pub_type: 杂志文章
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journal_title:Infection and immunity
pub_type: 杂志文章
doi:10.1128/IAI.66.10.5001-5007.1998
更新日期:1998-10-01 00:00:00
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journal_title:Infection and immunity
pub_type: 杂志文章
doi:
更新日期:1980-08-01 00:00:00
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journal_title:Infection and immunity
pub_type: 杂志文章
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