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1.
J Med Primatol ; 36(2): 61-79, 2007 Apr.
Article in English | MEDLINE | ID: mdl-17493137

ABSTRACT

BACKGROUND: There are several comprehensive reviews of spontaneous neoplasia in non-human primates that compile individual cases or small numbers of cases, but do not provide statistical analysis of tumor incidence, demographics, or epidemiology. METHODS: This paper reports all spontaneous neoplasms (n = 363) diagnosed over a 15-year period in a baboon colony with an average annual colony population of 4000. RESULTS: A total of 363 spontaneous neoplasms were diagnosed in 313 baboons: 77 cases were males (25%) and 236 were females (75%); ages ranged from 1 month to 33 years (mean 16.5, median 17). CONCLUSIONS: The organ systems affected in descending order of number of neoplasms were hematopoietic organs (n = 101, 28%), urogenital tract (n = 78, 21%), integument (n = 43, 12%), alimentary tract (n = 43, 12%), endocrine organs (n = 40, 11%), nervous system (n = 33, 9%), musculoskeletal system (n = 5, 1%), and respiratory system (n = 4, 1%). Malignant cases numbered 171 (47%); 192 (53%) cases were benign.


Subject(s)
Animals, Laboratory , Monkey Diseases/epidemiology , Neoplasms/veterinary , Papio , Animals , Female , Incidence , Male , Neoplasms/epidemiology , Texas/epidemiology
2.
Anal Chem ; 78(24): 8245-55, 2006 Dec 15.
Article in English | MEDLINE | ID: mdl-17165813

ABSTRACT

Llamas possess a class of unconventional immunoglobulins that have only heavy chains; unpaired heavy variable domains are responsible for antigen binding. These domains have previously been cloned and expressed as single domain antibodies (sdAbs); they comprise the smallest known antigen binding fragments. SdAbs have been shown to bind antigens at >90 degrees C and to refold after being denatured. To take advantage of the remarkable properties of sdAbs, we constructed a large, semisynthetic llama sdAb library. This library facilitated the rapid selection of binders to an array of biothreat targets. We selected sdAb specific for live vaccinia virus (a smallpox virus surrogate), hen egg lysozyme, cholera toxin, ricin, and staphylococcal enterotoxin B. The selected sdAb possessed high specificity as well as enhanced thermal stability in comparison to conventional IgG and scFv antibodies. We also determined equilibrium dissociation constants as well as demonstrated the use of several antitoxin sdAbs as effective capture and reporter molecules in sandwich assays on the Luminex instrument. The ability to rapidly select such rugged antibodies will enhance the reliability of immunoassays by extending shelf life and the capacity to function in hostile environments.


Subject(s)
Antibodies/chemistry , Antitoxins/chemistry , Antiviral Agents/chemistry , Camelids, New World/immunology , Immunoglobulin Heavy Chains/chemistry , Amino Acid Sequence , Animals , Antibodies/immunology , Antitoxins/immunology , Antiviral Agents/immunology , Binding Sites , Cholera Toxin/chemistry , Cholera Toxin/immunology , Enterotoxins/chemistry , Enterotoxins/immunology , Hot Temperature , Immunoglobulin Fragments/chemistry , Immunoglobulin Fragments/immunology , Immunoglobulin Heavy Chains/immunology , Immunoglobulin Variable Region/chemistry , Immunoglobulin Variable Region/immunology , Molecular Sequence Data , Muramidase/chemistry , Muramidase/immunology , Peptide Library , Ricin/chemistry , Ricin/immunology , Vaccinia virus/chemistry , Vaccinia virus/immunology
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