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OBJECTIVE: Simpatía, a term that captures the tendency to prefer and create social interactions characterized by warmth and emotional positivity while also avoiding conflict and/or overt negativity, is a cultural factor relevant to Latinos. The goal of this article was to develop a scale that measures this cultural value. METHOD: A self-report scale measure of simpatía was developed and administered to a combined sample of Latinos (N = 296) drawn from 3 larger studies. The scale's factor structure was explored, and its internal consistency and validity were tested. RESULTS: Exploratory factor analysis supported an 18-item scale and indicated 2 factors: simpatía-related positivity/warmth and simpatía-related negativity/conflict avoidance. Cronbach's alphas for the overall scale and subscales showed internal consistency. Validity analyses revealed that across subscales, simpatía was positively associated with positive emotion expressivity and dispositional positive emotion. The simpatía-related positivity/warmth subscale was also positively associated with an orientation toward Latino culture. CONCLUSIONS: The Simpatía Scale, which captures dual aspects of simpatía that emphasize the positive and avoid the negative, provides a new tool for advancing the study of Latino culture. (PsycInfo Database Record (c) 2020 APA, all rights reserved).
Assuntos
Hispânico ou Latino , Motivação , Análise Fatorial , Humanos , Relações Interpessoais , Psicometria , Reprodutibilidade dos Testes , Autorrelato , Inquéritos e QuestionáriosRESUMO
Chlamydia trachomatis, a leading cause of bacterial sexually transmitted infections, creates a specialized intracellular replicative niche by translocation and insertion of a diverse array of effectors (Incs [inclusion membrane proteins]) into the inclusion membrane. Here, we characterize IncE, a multifunctional Inc that encodes two non-overlapping short linear motifs (SLiMs) within its short cytosolic C terminus. The proximal SLiM, by mimicking just a small portion of an R-N-ethylmaleimide-sensitive factor adaptor protein receptor (SNARE) motif, binds and recruits syntaxin (STX)7- and STX12-containing vesicles to the inclusion. The distal SLiM mimics the sorting nexin (SNX)5 and SNX6 cargo binding site to recruit SNX6-containing vesicles to the inclusion. By simultaneously binding two distinct vesicle classes, IncE brings these vesicles in close apposition with each other at the inclusion to facilitate C. trachomatis intracellular development. Our work suggests that Incs may have evolved SLiMs to enable rapid evolution in a limited protein space to disrupt host cell processes.
RESUMO
Chlamydia trachomatis, a leading cause of bacteria sexually transmitted infections, creates a specialized intracellular replicative niche by translocation and insertion of a diverse array of effectors (Incs) into the inclusion membrane. Here, we characterize IncE, a multi-functional Inc that encodes two non-overlapping short linear motifs (SLiMs) within its short cytosolic C-terminus. The proximal SLiM mimics an R-SNARE motif to recruit syntaxin (STX) 7 and 12-containing vesicles to the inclusion. The distal SLiM mimics the Sorting Nexin (SNX) 5 and 6 cargo binding site to recruit SNX6-containing vesicles to the inclusion. By simultaneously binding to two distinct vesicle classes, IncE reprograms host cell trafficking to promote the formation of a class of hybrid vesicles at the inclusion that are required for C. trachomatis intracellular development. Our work suggests that Incs may have evolved SLiMs to facilitate rapid evolution in a limited protein space to disrupt host cell processes.
RESUMO
Chlamydia trachomatis is the leading cause of bacterial sexually transmitted infections in the USA and of preventable blindness worldwide. This obligate intracellular pathogen replicates within a membrane-bound inclusion, but how it acquires nutrients from the host while avoiding detection by the innate immune system is incompletely understood. C. trachomatis accomplishes this in part through the translocation of a unique set of effectors into the inclusion membrane, the inclusion membrane proteins (Incs). Incs are ideally positioned at the host-pathogen interface to reprogram host signaling by redirecting proteins or organelles to the inclusion. Using a combination of co-affinity purification, immunofluorescence confocal imaging, and proteomics, we characterize the interaction between an early-expressed Inc of unknown function, Tri1, and tumor necrosis factor receptor-associated factor 7 (TRAF7). TRAF7 is a multi-domain protein with a RING finger ubiquitin ligase domain and a C-terminal WD40 domain. TRAF7 regulates several innate immune signaling pathways associated with C. trachomatis infection and is mutated in a subset of tumors. We demonstrate that Tri1 and TRAF7 specifically interact during infection and that TRAF7 is recruited to the inclusion. We further show that the predicted coiled-coil domain of Tri1 is necessary to interact with the TRAF7 WD40 domain. Finally, we demonstrate that Tri1 displaces the native TRAF7 binding partners, mitogen-activated protein kinase kinase kinase 2 (MEKK2), and MEKK3. Together, our results suggest that by displacing TRAF7 native binding partners, Tri1 has the capacity to alter TRAF7 signaling during C. trachomatis infection.IMPORTANCEChlamydia trachomatis is the leading cause of bacterial sexually transmitted infections in the USA and preventable blindness worldwide. Although easily treated with antibiotics, the vast majority of infections are asymptomatic and therefore go untreated, leading to infertility and blindness. This obligate intracellular pathogen evades the immune response, which contributes to these outcomes. Here, we characterize the interaction between a C. trachomatis-secreted effector, Tri1, and a host protein involved in innate immune signaling, TRAF7. We identified host proteins that bind to TRAF7 and demonstrated that Tri1 can displace these proteins upon binding to TRAF7. Remarkably, the region of TRAF7 to which these host proteins bind is often mutated in a subset of human tumors. Our work suggests a mechanism by which Tri1 may alter TRAF7 signaling and has implications not only in the pathogenesis of C. trachomatis infections but also in understanding the role of TRAF7 in cancer.
Assuntos
Proteínas de Bactérias , Infecções por Chlamydia , Chlamydia trachomatis , Interações Hospedeiro-Patógeno , Humanos , Chlamydia trachomatis/metabolismo , Chlamydia trachomatis/genética , Chlamydia trachomatis/imunologia , Células HeLa , Proteínas de Bactérias/metabolismo , Proteínas de Bactérias/genética , Infecções por Chlamydia/microbiologia , Infecções por Chlamydia/metabolismo , Infecções por Chlamydia/imunologia , Transdução de Sinais , Peptídeos e Proteínas Associados a Receptores de Fatores de Necrose Tumoral/metabolismo , Peptídeos e Proteínas Associados a Receptores de Fatores de Necrose Tumoral/genética , Imunidade Inata , Ligação Proteica , Proteínas de Membrana/metabolismo , Proteínas de Membrana/genética , Células HEK293RESUMO
Chlamydia trachomatis is the leading cause of bacterial sexually transmitted infections in the US and of preventable blindness worldwide. This obligate intracellular pathogen replicates within a membrane-bound inclusion, but how it acquires nutrients from the host while avoiding detection by the innate immune system is incompletely understood. C. trachomatis accomplishes this in part through the translocation of a unique set of effectors into the inclusion membrane, the inc lusion membrane proteins (Incs). Incs are ideally positioned at the host-pathogen interface to reprogram host signaling by redirecting proteins or organelles to the inclusion. Using a combination of co-affinity purification, immunofluorescence confocal imaging, and proteomics, we characterize the interaction between an early-expressed Inc of unknown function, Tri1, and tumor necrosis factor receptor associated factor 7 (TRAF7). TRAF7 is a multi-domain protein with a RING finger ubiquitin ligase domain and a C-terminal WD40 domain. TRAF7 regulates several innate immune signaling pathways associated with C. trachomatis infection and is mutated in a subset of tumors. We demonstrate that Tri1 and TRAF7 specifically interact during infection and that TRAF7 is recruited to the inclusion. We further show that the predicted coiled-coil domain of Tri1 is necessary to interact with the TRAF7 WD40 domain. Finally, we demonstrate that Tri1 displaces the native TRAF7 binding partners, mitogen activated protein kinase kinase kinase 2 (MEKK2) and MEKK3. Together, our results suggest that by displacing TRAF7 native binding partners, Tri1 has the capacity to alter TRAF7 signaling during C. trachomatis infection. Importance: Chlamydia trachomatis is the leading cause of bacterial sexually transmitted infections in the US and preventable blindness worldwide. Although easily treated with antibiotics, the vast majority of infections are asymptomatic and therefore go untreated, leading to infertility and blindness. This obligate intracellular pathogen evades the immune response, which contributes to these outcomes. Here, we characterize the interaction between a C. trachomatis secreted effector, Tri1, and a host protein involved in innate immune signaling, TRAF7. We identified host proteins that bind to TRAF7 and demonstrate that Tri1 can displace these proteins upon binding to TRAF7. Remarkably, the region of TRAF7 to which these host proteins bind is often mutated in a subset of human tumors. Our work suggests a mechanism by which Tri1 may alter TRAF7 signaling and has implications not only in the pathogenesis of C. trachomatis infections, but also in understanding the role of TRAF7 in cancer.
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PGAM5 is a mitochondrial protein phosphatase whose genetic ablation in mice results in mitochondria-related disorders, including neurodegeneration. Functions of PGAM5 include regulation of mitophagy, cell death, metabolism and aging. However, mechanisms regulating PGAM5 activation and signaling are poorly understood. Using electron cryo-microscopy, we show that PGAM5 forms dodecamers in solution. We also present a crystal structure of PGAM5 that reveals the determinants of dodecamer formation. Furthermore, we observe PGAM5 dodecamer assembly into filaments both in vitro and in cells. We find that PGAM5 oligomerization into a dodecamer is not only essential for catalytic activation, but this form also plays a structural role on mitochondrial membranes, which is independent of phosphatase activity. Together, these findings suggest that modulation of the oligomerization of PGAM5 may be a regulatory switch of potential therapeutic interest.
Assuntos
Microscopia Crioeletrônica/métodos , Fosfoproteínas Fosfatases/metabolismo , Fosfoproteínas Fosfatases/ultraestrutura , Animais , Morte Celular/genética , Morte Celular/fisiologia , Camundongos , Membranas Mitocondriais/metabolismo , Membranas Mitocondriais/ultraestrutura , Mitofagia/genética , Mitofagia/fisiologia , PolimerizaçãoRESUMO
Se evaluó la técnica de contrainmunoelectroforesis (CIE) para el diagnóstico serológico de la leptospirosis, utilizando un preparado antigénico de la cepa leptospira biflexa Patoc I. El estudio demostró que la técnica de CIE, presentó una sensibilidad del 82 por ciento y una especificidad del 100 por ciento. El antígeno empleado mostró una reactividad específica del género al detectar anticuerpos en pacientes infectados por distintos serogrupos de leptospira, mediante la prueba de microaglutinación (MA). La estabilidad del antígeno para la técnica de CIE fue de 6 meses sin pérdida de título
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Humanos , Masculino , Feminino , Imunoeletroforese , Leptospira/classificação , Leptospirose/diagnóstico , Testes de Sensibilidade Microbiana , SorologiaRESUMO
Se evaluó la técnica de contrainmunoelectroforesis (CIE) para el diagnóstico serológico de la leptospirosis, utilizando un preparado antigénico de la cepa Leptospira bifleza Patoc I. El estudio demostró que la técnica de CIE presentó una sensibilidad del 82 por ciento y una especificidad del 100 por ciento . El antígeno empleado mostró una reactividad específica de género al detectar anticuerpos en pacientes infectados por distintos serogrupos de leptospira, mediante la prueba de microaglutinación (MA). La estabilidad del antígeno para la técnica de CIE fue de 6 meses sin pérdida de título