ABSTRACT
Laboratory Response Network (LRN) laboratories help protect populations from biological and chemical public health threats. We examined the role of LRN biological laboratories in enhancing capacity to detect and respond to public health infectious disease emergencies in South Korea. The model for responding to infectious disease emergencies leverages standardized laboratory testing procedures, a repository of standardized testing reagents, laboratory testing cooperation among hospital sentinel laboratories and reference laboratories, and maintenance of a trained workforce through traditional and on-demand training. Cooperation among all network stakeholders helps ensure that laboratory response is an integrated part of the national response. The added laboratory testing capacity provided by the US Centers for Disease Control and Prevention LRN assets helps protect persons who reside in South Korea, US military personnel and civilians in South Korea, and those who reside in the continental United States.
Subject(s)
Capacity Building , Communicable Diseases/epidemiology , Disease Outbreaks , Laboratories , Capacity Building/methods , Capacity Building/organization & administration , Emergencies , Humans , Laboratories/organization & administration , Laboratories/statistics & numerical data , Microbiology/organization & administration , Republic of Korea , Sentinel Surveillance , WorkforceSubject(s)
Bacillus anthracis/genetics , Bacillus anthracis/isolation & purification , Polymerase Chain Reaction/methods , Animals , Anthrax/diagnosis , Anthrax/microbiology , Bacillus anthracis/classification , Bioterrorism , Environmental Monitoring , Genes, Bacterial , Genotype , Humans , Reproducibility of Results , Sensitivity and Specificity , Time FactorsABSTRACT
A monoclonal antibody (MAb) directed against an unknown Chlamydophila pneumoniae epitope has been characterized, and the respective peptide mimotope has been identified. A murine MAb specific for C. pneumoniae was used to select peptides from phage display libraries. The peptides identified from the phage display library clones reacted specifically with the respective target murine MAb and with human sera previously identified as having antibody titers to C. pneumoniae. The selected peptide mimotope sequences tended to be composed of charged residues surrounding a core of hydrophobic residues. The peptide with the best binding could inhibit >95% of binding to the MAb, suggesting that the selected peptide binds the paratope of the respective MAb. The peptide reacted with human sera previously determined by microimmunofluorescence to have anti-C. pneumoniae antibodies. The peptide was competitively competed with the MAb against Renografin-purified, sonicated C. pneumoniae in an enzyme-linked immunosorbent assay and with whole-cell C. pneumoniae in an indirect fluorescence assay format, demonstrating its potential utility in the development of diagnostics. The use of this novel peptide may allow investigators to establish standardized assays free from cross-reactive Chlamydia trachomatis and Chlamydophila psittaci epitopes and immunoreactivity.
