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1.
Acta Trop ; 242: 106907, 2023 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-36963599

RESUMO

The taeniasis/cysticercosis complex (TCC) belongs to the group of neglected infectious diseases with a multifactorial transmission that includes hosts such as humans and pigs of the parasitic tapeworm (Taenia solium) and environmental factors. This study represents the first phase of the National and Cross-sectoral Plan for TCC Elimination. OBJECTIVES: To obtain data about knowledge and practices in relation to the TCC from knowledge, attitudes, and practices (KAP) surveys applied in two pilot localities for building a baseline of the potential risk factors related to identification, prevention, and control of TCC in Colombia. METHODS: A descriptive cross-sectional survey from October to November in 2019 was carried out using a structured questionnaire and random sampling by single-stage conglomerates in the municipalities of Mahates, Bolívar (n = 152) (Atlantic Region) and Mercaderes, Cauca (n = 152) (Andean Region). RESULTS: Respondents in Mahates showed moderate knowledge about TCC compared to those in Mercaderes, however, risky practices were identified in both places (consumption of pork with cysts and defecation in places other than the bathroom or latrine). Deficiency in infrastructure and failure in basic services were observed as potential risk factors for TCC transmission in both municipalities. CONCLUSION: Based on the framework of the National and Cross-sectoral Plan for TCC Elimination, adequate knowledge on identification, prevention, and control of the disease must be reinforced; cultural and ecological differences should be considered when designing communication and knowledge transmission tools. We consider that major investment should be made in improving basic services and creating sustainable modernized pig farming in Mahates and Mercaderes.


Assuntos
Cisticercose , Doenças dos Suínos , Taenia solium , Teníase , Humanos , Animais , Suínos , Colômbia , Estudos Transversais , Cisticercose/prevenção & controle , Teníase/parasitologia , Doenças dos Suínos/prevenção & controle , Doenças dos Suínos/parasitologia
2.
Biochim Biophys Acta Proteins Proteom ; 1865(11 Pt A): 1423-1432, 2017 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-28803140

RESUMO

The protozoan parasite Trichomonas vaginalis contains two nearly identical triosephosphate isomerases (TvTIMs) that dissociate into stable monomers and dimerize upon substrate binding. Herein, we compare the role of the "ball and socket" and loop 3 interactions in substrate assisted dimer assembly in both TvTIMs. We found that point mutants at the "ball" are only 39 and 29-fold less catalytically active than their corresponding wild-type counterparts, whereas Δloop 3 deletions are 1502 and 9400-fold less active. Point and deletion mutants dissociate into stable monomers. However, point mutants assemble as catalytic competent dimers upon binding of the transition state substrate analog PGH, whereas loop 3 deletions remain monomeric. A comparison between crystal structures of point and loop 3 deletion monomeric mutants illustrates that the catalytic residues in point mutants and wild-type TvTIMs are maintained in the same orientation, whereas the catalytic residues in deletion mutants show an increase in thermal mobility and present structural disorder that may hamper their catalytic role. The high enzymatic activity present in monomeric point mutants correlates with the formation of dimeric TvTIMs upon substrate binding. In contrast, the low activity and lack of dimer assembly in deletion mutants suggests a role of loop 3 in promoting the formation of the active site as well as dimer assembly. Our results suggest that in TvTIMs the active site is assembled during dimerization and that the integrity of loop 3 and ball and socket residues is crucial to stabilize the dimer.


Assuntos
Sequência de Bases , Ácidos Hidroxâmicos/química , Proteínas de Protozoários/química , Deleção de Sequência , Trichomonas vaginalis/enzimologia , Triose-Fosfato Isomerase/química , Motivos de Aminoácidos , Domínio Catalítico , Cristalografia por Raios X , Escherichia coli/genética , Escherichia coli/metabolismo , Expressão Gênica , Teste de Complementação Genética , Ácidos Hidroxâmicos/metabolismo , Cinética , Modelos Moleculares , Mutação Puntual , Ligação Proteica , Domínios e Motivos de Interação entre Proteínas , Multimerização Proteica , Estrutura Secundária de Proteína , Proteínas de Protozoários/genética , Proteínas de Protozoários/metabolismo , Proteínas Recombinantes/química , Proteínas Recombinantes/genética , Proteínas Recombinantes/metabolismo , Especificidade por Substrato , Termodinâmica , Trichomonas vaginalis/química , Triose-Fosfato Isomerase/genética , Triose-Fosfato Isomerase/metabolismo
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