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1.
QJM ; 117(3): 231-232, 2024 Mar 27.
Artigo em Inglês | MEDLINE | ID: mdl-38039181
3.
6.
Epidemiol Infect ; 131(3): 1049-54, 2003 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-14959769

RESUMO

In winter 2001, an outbreak of pertussis involving an estimated 75 people occurred among soldiers serving in an infantry regiment of the Israeli Defense Forces (IDF). Nasopharyngeal swabs were obtained from patients and contacts for culture and PCR. Serum samples were obtained and assayed by ELISA for the presence of IgA, IgM and IgG antibodies to a lysate antigen of Bordetella pertussis. The calculated attack rate was 21% based on clinical signs alone (cough lasting 30 days or longer) and 9.5% based on clinical signs with laboratory confirmation (by PCR, IgA or IgM). A high carriage rate was observed; 20% of the asymptomatic and previously symptomatic subjects were PCR-positive for B. pertussis. These findings emphasize the importance of B. pertussis as a causative agent of epidemic respiratory infections in young adults and reveal the occurrence of a significant proportion of pertussis transient carriers during an outbreak of the disease.


Assuntos
Surtos de Doenças , Militares , Coqueluche/epidemiologia , Adulto , Bordetella pertussis/genética , Bordetella pertussis/imunologia , Bordetella pertussis/patogenicidade , Portador Sadio , Ensaio de Imunoadsorção Enzimática , Feminino , Humanos , Imunoglobulina A/análise , Imunoglobulina G/análise , Imunoglobulina M/análise , Israel/epidemiologia , Masculino , Nasofaringe/microbiologia , Vacina contra Coqueluche , Reação em Cadeia da Polimerase , Coqueluche/imunologia
7.
J Biol Chem ; 275(42): 33134-41, 2000 Oct 20.
Artigo em Inglês | MEDLINE | ID: mdl-10924524

RESUMO

Hairpin and tetrahelical structures of a d(CGG)(n) sequence in the FMR1 gene have been implicated in its expansion in fragile X syndrome. The identification of tetraplex d(CGG)(n) destabilizing proteins (Fry, M., and Loeb, L. A.(1999) J. Biol. Chem. 274, 12797-12803; Weisman-Shomer, P., Naot, Y., and Fry, M. (2000) J. Biol. Chem. 275, 2231-2238) suggested that proteins might modulate d(CGG)(n) folding and aggregation. We assayed human TK-6 lymphoblastoid cell extracts for d(CGG)(8) oligomer binding proteins. The principal binding protein was identified as Ku antigen by its partial amino acid sequence and antigenicity. The purified 88/75-kDa heterodimeric Ku bound with similar affinities (K(d) approximately 1. 8-10.2 x 10(-9) mol/liter) to double-stranded d(CGG)(8).d(CCG)(8), hairpin d(CGG)(8), single-stranded d(CII)(8), or tetraplex structures of telomeric or IgG switch region sequences. However, Ku associated more tightly with bimolecular G'2 tetraplex d(CGG)(8) (K(d) approximately 0.35 x 10(-9) mol/liter). Binding to Ku protected G'2 d(CGG)(8) against nuclease digestion and impeded its unwinding by the tetraplex destabilizing protein qTBP42. Stabilization of d(CGG)(n) tetraplex domains in FMR1 by Ku or other proteins might promote d(CGG) expansion and FMR1 silencing.


Assuntos
Antígenos Nucleares , DNA Helicases , Proteínas de Ligação a DNA/metabolismo , DNA/química , DNA/genética , Síndrome do Cromossomo X Frágil/genética , Proteínas Nucleares/metabolismo , Conformação de Ácido Nucleico , Expansão das Repetições de Trinucleotídeos , Sequência de Aminoácidos , Sequência de Bases , Sítios de Ligação , Proteínas de Ligação a DNA/química , Humanos , Cinética , Autoantígeno Ku , Dados de Sequência Molecular , Proteínas Nucleares/química , Oligodesoxirribonucleotídeos/química , Oligodesoxirribonucleotídeos/metabolismo , Fatores de Transcrição/metabolismo
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