Editing Anthrax (section)

=== Biologic for Drug-, Antibody- or Vaccine-resistant Anthrax ===
Treatment of multi-drug resistant, antibody- or vaccine-resistant Anthrax is also possible.  Legler, et al.<ref>{{cite journal | vauthors = Legler PM, Little SF, Senft J, Schokman R, Carra JH, Compton JR, Chabot D, Tobery S, Fetterer DP, Siegel JB, Baker D, Friedlander AM | title = Treatment of experimental anthrax with pegylated circularly permuted capsule depolymerase | journal = Science Translational Medicine | volume = 13 | issue = 623 | pages = eabh1682 | date = December 2021 | pmid = 34878819 | doi = 10.1126/scitranslmed.abh1682 }}</ref> showed that pegylated CapD (capsule depolymerase) could provide protection against 5 LD50 exposures to lethal Ames spores without the use of antibiotics, monoclonal antibodies, or vaccines.  The CapD enzyme removes the poly-D-glutamate (PDGA) capsular material from the bacteria, rendering it susceptible to the innate immune responses.  The unencapsulated bacteria can then be cleared.<ref>{{YouTube|id=QVSM2vaTFaE|title=Engineered enzyme against antibiotic resistant anthrax}}</ref>

[[File:CapD.jpg|thumb|center|400px|''B. anthracis'' Capsule Depolymerase (CapD) degrades the unusual PDGA capsule on the outer surface of the bacterium. The pegylated enzyme has been used in mice to protect against five LD50 challenges of lethal Ames spores.<ref name="pmid22257032">{{cite journal | vauthors = Hu X, Legler PM, Khavrutskii I, Scorpio A, Compton JR, Robertson KL, Friedlander AM, Wallqvist A | title = Probing the donor and acceptor substrate specificity of the γ-glutamyl transpeptidase | journal = Biochemistry | volume = 51 | issue = 6 | pages = 1199–1212 | date = February 2012 | pmid = 22257032 | doi = 10.1021/bi200987b }}</ref> The human enzyme (white surface) has been overlaid onto the bacterial CapD structure (PDB 3G9K,<ref name="Joachimiak">{{cite journal | vauthors = Wu R, Richter S, Zhang RG, Anderson VJ, Missiakas D, Joachimiak A | title = Crystal structure of Bacillus anthracis transpeptidase enzyme CapD | journal = The Journal of Biological Chemistry | volume = 284 | issue = 36 | pages = 24406–24414 | date = September 2009 | pmid = 19535342 | pmc = 2782033 | doi = 10.1074/jbc.M109.019034 | doi-access = free }}</ref> blue ribbon). In red is the substrate binding loop of HuGGT which CapD lacks. CapD binds polymers of D-glutamate. Original figure from Hu, Legler, et al.<ref name="pmid22257032" />]]