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1.
Parasite Immunol ; 35(12): 409-20, 2013 Dec.
Artículo en Inglés | MEDLINE | ID: mdl-23834512

RESUMEN

Leishmania major is an aetiological agent of cutaneous leishmaniasis. The parasite primarily infects immune sentinel cells, specifically macrophages and dendritic cells, in the mammalian host. Infection is receptor mediated and is known to involve parasite binding to cell surface protein complement receptor 3 (CR3, Mac-1, CD11b/CD18). Engagement of CR3 by various ligands inhibits production of interleukin-12 (IL-12), the cytokine that drives antileishmanial T helper 1-type immune responses. Likewise, L. major infection inhibits IL-12 production and activation of host macrophages. Our data indicate that in the absence of CR3, L. major-infected bone marrow-derived macrophages produce more IL-12 and nitric oxide compared with WT cells upon lipopolysaccharide (LPS) stimulation. We therefore investigated multiple signalling pathways by which L. major may inhibit IL-12 transcription through CR3 ligation. We demonstrate that L. major infection does not elicit significant NFκB p65, MAPK, IRF-1 or IRF-8 activation in WT or CD11b-deficient macrophages. Furthermore, infection neither inhibits LPS-induced MAPK or NFκB activation nor blocks IFN-γ-activated IRF-1 and IRF-8. ETS-mediated transcription, however, is inhibited by L. major infection independently of CR3. Our data indicate that L. major-mediated inhibition of IL-12 occurs through CR3 engagement; however, the mechanism of inhibition is independent of NFκB, MAPK, IRF and ETS.


Asunto(s)
Interleucina-12/genética , Leishmania major/inmunología , Leishmania major/fisiología , Leishmaniasis Cutánea/inmunología , Antígeno de Macrófago-1/metabolismo , Macrófagos/inmunología , Macrófagos/parasitología , Transcripción Genética , Animales , Regulación hacia Abajo , Regulación de la Expresión Génica , Factor 1 Regulador del Interferón/metabolismo , Factores Reguladores del Interferón/metabolismo , Interleucina-12/biosíntesis , Interleucina-12/inmunología , Leishmania major/genética , Leishmaniasis Cutánea/genética , Leishmaniasis Cutánea/metabolismo , Leishmaniasis Cutánea/parasitología , Lipopolisacáridos/inmunología , Antígeno de Macrófago-1/genética , Antígeno de Macrófago-1/inmunología , Macrófagos/metabolismo , Ratones , Ratones Endogámicos BALB C , Proteínas Quinasas Activadas por Mitógenos/metabolismo , FN-kappa B/metabolismo , Óxido Nítrico/metabolismo , Transducción de Señal
2.
Science ; 277(5329): 1091-3, 1997 Aug 22.
Artículo en Inglés | MEDLINE | ID: mdl-9262476

RESUMEN

Tuberculosis is the leading cause of death due to an infectious organism, killing an estimated 3 million people annually. Mycobacterium tuberculosis, the causative agent of tuberculosis, and other pathogenic mycobacteria require entry into host macrophages to initiate infection. An invasion mechanism was defined that was shared among pathogenic mycobacteria including M. tuberculosis, M. leprae, and M. avium but not by nonpathogenic mycobacteria or nonmycobacterial intramacrophage pathogens. This pathway required the association of the complement cleavage product C2a with mycobacteria resulting in the formation of a C3 convertase. The mycobacteria-associated C2a cleaved C3, resulting in C3b opsonization of the mycobacteria and recognition by macrophages.


Asunto(s)
Complemento C2/fisiología , Macrófagos/microbiología , Complejo Mycobacterium avium/patogenicidad , Mycobacterium/patogenicidad , Secuencia de Aminoácidos , Animales , Complemento C2a , Complemento C3/metabolismo , Convertasas de Complemento C3-C5/metabolismo , Complemento C3b/inmunología , Caballos , Humanos , Técnicas In Vitro , Isoflurofato/farmacología , Macrófagos/inmunología , Ratones , Datos de Secuencia Molecular , Complejo Mycobacterium avium/inmunología , Mycobacterium bovis/inmunología , Mycobacterium bovis/patogenicidad , Mycobacterium leprae/inmunología , Mycobacterium leprae/patogenicidad , Mycobacterium tuberculosis/inmunología , Mycobacterium tuberculosis/patogenicidad , Proteínas Opsoninas , Virulencia
3.
EBioMedicine ; 25: 112-121, 2017 Nov.
Artículo en Inglés | MEDLINE | ID: mdl-29100778

RESUMEN

More efficacious treatment regimens are needed for tuberculosis, however, drug development is impeded by a lack of reliable biomarkers of disease severity and of treatment effect. We conducted a directed screen of host biomarkers in participants enrolled in a tuberculosis clinical trial to address this need. Serum samples from 319 protocol-correct, culture-confirmed pulmonary tuberculosis patients treated under direct observation as part of an international, phase 2 trial were screened for 70 markers of infection, inflammation, and metabolism. Biomarker assays were specifically developed for this study and quantified using a novel, multiplexed electrochemiluminescence assay. We evaluated the association of biomarkers with baseline characteristics, as well as with detailed microbiologic data, using Bonferroni-adjusted, linear regression models. Across numerous analyses, seven proteins, SAA1, PCT, IL-1ß, IL-6, CRP, PTX-3 and MMP-8, showed recurring strong associations with markers of baseline disease severity, smear grade and cavitation; were strongly modulated by tuberculosis treatment; and had responses that were greater for patients who culture-converted at 8weeks. With treatment, all proteins decreased, except for osteocalcin, MCP-1 and MCP-4, which significantly increased. Several previously reported putative tuberculosis-associated biomarkers (HOMX1, neopterin, and cathelicidin) were not significantly associated with treatment response. In conclusion, across a geographically diverse and large population of tuberculosis patients enrolled in a clinical trial, several previously reported putative biomarkers were not significantly associated with treatment response, however, seven proteins had recurring strong associations with baseline radiographic and microbiologic measures of disease severity, as well as with early treatment response, deserving additional study.


Asunto(s)
Biomarcadores/sangre , Índice de Severidad de la Enfermedad , Tuberculosis Pulmonar/sangre , Tuberculosis Pulmonar/tratamiento farmacológico , Adulto , Anciano , Antituberculosos , Combinación de Medicamentos , Etambutol/administración & dosificación , Femenino , Humanos , Isoniazida/administración & dosificación , Masculino , Persona de Mediana Edad , Pirazinamida/administración & dosificación , Rifampin/administración & dosificación , Resultado del Tratamiento , Tuberculosis Pulmonar/patología
6.
Curr Drug Targets ; 9(2): 123-9, 2008 Feb.
Artículo en Inglés | MEDLINE | ID: mdl-18288963

RESUMEN

The ability of the innate immune system to quickly recognize and respond to an invading pathogen is essential for controlling the infection. For this purpose, cells of the immune system express receptors which recognize evolutionarily conserved structures expressed by various pathogens but absent from host cells. In this review we focus on the non-classical C-type lectin receptors including Dectin-1 whose role has been extensively characterized in the recognition and response to fungal pathogens. Dectin-1 is a type II transmembrane protein which binds beta-1,3 and beta-1,6 glucans. It is expressed on most cells of the innate immune system and has been implicated in phagocytosis as well as killing of fungi by macrophages, neutrophils and dendritic cells. The Dectin-1 cytoplasmic tail contains an immunoreceptor tyrosine based activation motif (ITAM) that signals in part through the spleen tyrosine kinase and in collaboration with Toll-like receptors. Although the main research focus has been on Dectin-1's role as a fungal and yeast pathogen recognition receptor, more recent studies suggest that Dectin-1 may have a broader function in pathogen recognition including a role in directing a macrophage response to mycobacterial infections.


Asunto(s)
Proteínas de la Membrana/inmunología , Proteínas del Tejido Nervioso/inmunología , Receptores de Reconocimiento de Patrones/inmunología , Animales , Hongos/inmunología , Humanos , Inmunidad Innata/inmunología , Lectinas Tipo C , Macrófagos/inmunología , Proteínas de la Membrana/metabolismo , Mycobacterium/inmunología , Proteínas del Tejido Nervioso/metabolismo , Fagocitosis/inmunología , Receptores de Reconocimiento de Patrones/metabolismo , Transducción de Señal
7.
J Cell Sci ; 108 ( Pt 5): 2001-6, 1995 May.
Artículo en Inglés | MEDLINE | ID: mdl-7657720

RESUMEN

Human procathepsin D carries two N-linked glycosylation sites at asparagine residues 70 and 199, widely separated on the surface of the folded protein. We created monoglycosylated procathepsin D molecules by site-directed mutagenesis in vitro of the individual glycosylation sites. With only two exceptions, all 12 mutants of this type were expressed efficiently in mammalian cells. The expressed proteins were stable, targeted to the lysosome, and partially secreted into the medium. When both glycosylation sites were eliminated, however, the expressed proteins (9 different mutants) were stable but most were not secreted and targeted poorly to the lysosome. Mammalian fibroblasts appear to sort nascent procathepsin D efficiently only if it is N-glycosylated. Procathepsin D monoglycosylated at N70 is readily distinguished from the endogenous protein in transfected human cells and thus provides an excellent substrate for studying lysosomal targeting in an homologous system.


Asunto(s)
Catepsina D/metabolismo , Precursores Enzimáticos/metabolismo , Proteínas de Choque Térmico , Procesamiento Proteico-Postraduccional , Animales , Células CHO , Proteínas Portadoras/genética , Proteínas Portadoras/metabolismo , Catepsina D/genética , Compartimento Celular , Cricetinae , Cricetulus , ADN Complementario/genética , Chaperón BiP del Retículo Endoplásmico , Precursores Enzimáticos/genética , Fibroblastos/metabolismo , Glicosilación , Humanos , Lisosomas/metabolismo , Chaperonas Moleculares/genética , Chaperonas Moleculares/metabolismo , Mutagénesis Sitio-Dirigida , Proteínas Proto-Oncogénicas c-myc/genética , Proteínas Proto-Oncogénicas c-myc/metabolismo , Proteínas Recombinantes de Fusión/metabolismo , Especificidad de la Especie , Transfección
8.
J Cell Sci ; 108 ( Pt 5): 2007-15, 1995 May.
Artículo en Inglés | MEDLINE | ID: mdl-7657721

RESUMEN

A major pathway to the lysosome for soluble hydrolases involves the 6-phosphorylation of mannose residues. The initial step in this reaction is catalyzed by a phosphotransferase which recognizes lysosomal precursors. We constructed mutants of human procathepsin D whose targeting to the lysosome could be assayed directly in intact cells. Eight lysine residues were individually converted to glutamic acid on the surface of the carboxyl terminal lobe of the protein. Mutants with as many as four Lys to Glu mutations were normally targeted to the lysosome and processed to the mature form of the enzyme in transfected cells. We conclude that the C-terminal lobe of procathepsin D may not carry a determinant essential for lysosomal targeting in intact fibroblasts.


Asunto(s)
Catepsina D/metabolismo , Precursores Enzimáticos/metabolismo , Lisina , Lisosomas/metabolismo , Procesamiento Proteico-Postraduccional , Estructura Terciaria de Proteína , Proteínas Recombinantes de Fusión/metabolismo , Animales , Transporte Biológico , Células CHO , Catepsina D/química , Catepsina D/genética , Línea Celular Transformada , Chlorocebus aethiops , Cricetinae , Cricetulus , Precursores Enzimáticos/química , Precursores Enzimáticos/genética , Femenino , Glicosilación , Humanos , Manosafosfatos/metabolismo , Mutagénesis Sitio-Dirigida , Fosforilación , Fosfotransferasas/metabolismo , Proteínas Proto-Oncogénicas c-myc/genética , Proteínas Proto-Oncogénicas c-myc/inmunología , Renina/metabolismo , Especificidad de la Especie
9.
J Immunol ; 163(4): 1775-85, 1999 Aug 15.
Artículo en Inglés | MEDLINE | ID: mdl-10438909

RESUMEN

NK cells are most effective in killing a broad spectrum of primary tumor cells after stimulation with cytokines. We have cloned a novel gene, designated NKLAM (for NK lytic-associated molecule), whose expression is associated with this cytokine-enhanced process. NKLAM expression is up-regulated in NK cells by IL-2 and IFN-beta. NKLAM is also selectively expressed by activated macrophages and CTL. Treatment of NK cells and CTL with NKLAM antisense oligonucleotides specifically decreases their cytolytic activity, while having no effect on cell growth. The NKLAM gene encodes a 62-kDa ring finger-containing protein that localizes to the cytoplasmic granules in NK cells. Further study of this gene may add to our understanding of cytotoxic processes common to NK cells, CTL, and activated macrophages.


Asunto(s)
Citotoxicidad Inmunológica/genética , Regulación de la Expresión Génica/inmunología , Células Asesinas Naturales/metabolismo , Proteínas de la Membrana/biosíntesis , Proteínas de la Membrana/genética , Secuencia de Aminoácidos , Animales , Línea Celular , Células Clonales , Gránulos Citoplasmáticos/enzimología , Gránulos Citoplasmáticos/inmunología , Granzimas , Humanos , Interferón beta/farmacología , Células Asesinas Naturales/inmunología , Leucocitos Mononucleares/metabolismo , Activación de Linfocitos/genética , Proteínas de la Membrana/química , Proteínas de la Membrana/inmunología , Ratones , Datos de Secuencia Molecular , Homología de Secuencia de Aminoácido , Serina Endopeptidasas/metabolismo , Células Tumorales Cultivadas , Dedos de Zinc/genética , Dedos de Zinc/inmunología
10.
Infect Immun ; 69(12): 7729-35, 2001 Dec.
Artículo en Inglés | MEDLINE | ID: mdl-11705954

RESUMEN

We investigated the importance of the host complement system in the pathogenesis of disease mediated by the intramacrophage pathogen Mycobacterium avium. Mycobacteria opsonized with complement are efficiently ingested by macrophages through various complement receptors. Furthermore, unlike other bacteria, mycobacteria can activate both the alternative and classical complement pathways in the absence of specific antibodies. Therefore, to examine the role of complement in the mycobacterial infection process in vivo, mice deficient in complement component C3 were infected with M. avium. Surprisingly, C3-deficient mice infected intravenously with M. avium displayed no difference in bacterial burden or granulomatous response compared to wild-type control mice. C3-sufficient mice and C3-deficient mice were equally susceptible to infection by M. avium regardless of the genotype at the bcg locus, a locus known to confer susceptibility to infection with intracellular pathogens. In vitro studies using mouse bone marrow-derived macrophages resulted in significant M. avium invasion of macrophages in the absence of C3; however, the kinetics of infection were delayed compared to complement-mediated invasion. The data indicate that complement does not play an essential role in mediating M. avium infections in the mouse and suggest either that other invasion mechanisms can compensate for the absence of complement-mediated entry or that complement is not a major mycobacterial opsonin in vivo.


Asunto(s)
Complemento C3/deficiencia , Mycobacterium avium/inmunología , Tuberculosis/etiología , Tuberculosis/inmunología , Animales , Anticuerpos Antibacterianos , Especificidad de Anticuerpos , Células de la Médula Ósea/inmunología , Vía Alternativa del Complemento , Vía Clásica del Complemento , Susceptibilidad a Enfermedades , Granuloma/etiología , Hígado/microbiología , Hígado/patología , Macrófagos/inmunología , Ratones , Ratones Mutantes , Proteínas Opsoninas , Bazo/microbiología , Factor de Necrosis Tumoral alfa/biosíntesis
11.
Infect Immun ; 66(3): 1261-4, 1998 Mar.
Artículo en Inglés | MEDLINE | ID: mdl-9488424

RESUMEN

The T-cell response to fibronectin attachment protein (FAP-A) in BALB/c and B10.BR mice was examined. Both strains developed strong T-cell responses to FAP-A, directed to single, unique epitopes. T cells from mice infected with Mycobacterium avium responded to FAP-A, suggesting a possible role in a protective immune response.


Asunto(s)
Adhesinas Bacterianas , Proteínas Bacterianas/inmunología , Proteínas Portadoras/inmunología , Epítopos , Activación de Linfocitos , Mycobacterium tuberculosis/inmunología , Linfocitos T/inmunología , Secuencia de Aminoácidos , Animales , Ratones , Ratones Endogámicos BALB C , Datos de Secuencia Molecular
12.
Mol Microbiol ; 21(2): 321-9, 1996 Jul.
Artículo en Inglés | MEDLINE | ID: mdl-8858587

RESUMEN

Mycobacterium avium is an intracellular pathogen and a major opportunistic infectious agent observed in patients with acquired immune deficiency syndrome (AIDS). Evidence suggests that the initial portal of infection by M. avium is often the gastrointestinal tract. However, the mechanism by which the M. avium crosses the epithelial barrier is unclear. A possible mechanism is suggested by the ability of M. avium to bind fibronectin, an extracellular matrix protein that is a virulence factor for several extracellular pathogenic bacteria which bind to mucosal surfaces. To further characterize fibronectin binding by M. avium, we have cloned the M. avium fibronectin-attachment protein (FAP). The M. avium FAP (FAP-A) has an unusually large number of Pro and Ala residues (40% overall) and is 50% identical to FAP of both Mycobacterium leprae and Mycobacterium tuberculosis. Using recombinant FAP-A and FAP-A peptides, we show that two non-continuous regions in FAP-A bind fibronectin. Peptides from these regions and homologous sequences from M. leprae FAP inhibit fibronectin binding by both M. avium and Mycobacterium bovis Bacillus Calmette-Guerin (BCG). These regions have no homology to eukaryotic fibronectin-binding proteins and are only distantly related to fibronectin-binding peptides of Gram-positive bacteria. Nevertheless, these fibronectin-binding regions are highly conserved among the mycobacterial FAPs, suggesting an essential function for this interaction in mycobacteria infection of their metazoan hosts.


Asunto(s)
Fibronectinas/metabolismo , Complejo Mycobacterium avium/genética , Complejo Mycobacterium avium/metabolismo , Mycobacterium/genética , Mycobacterium/metabolismo , Oligopéptidos/genética , Oligopéptidos/metabolismo , Infecciones Oportunistas Relacionadas con el SIDA/etiología , Secuencia de Aminoácidos , Sitios de Unión/genética , Clonación Molecular , Secuencia Conservada , Humanos , Datos de Secuencia Molecular , Complejo Mycobacterium avium/patogenicidad , Infección por Mycobacterium avium-intracellulare/etiología , Mycobacterium bovis/metabolismo , Unión Proteica , Homología de Secuencia de Aminoácido , Especificidad de la Especie
13.
Int J Cancer ; 86(1): 83-8, 2000 Apr 01.
Artículo en Inglés | MEDLINE | ID: mdl-10728599

RESUMEN

Intravesical Mycobacterium bovis bacillus Calmette-Gu*erin (BCG) is the treatment of choice for superficial bladder cancer. Previous studies showed that attachment of BCG to fibronectin within the bladder was necessary for mediation of the antitumor response. Further studies identified a bacterial receptor, fibronectin attachment protein (FAP), as an important mediator of BCG attachment to fibronectin. In vitro studies showed that a stable BCG/fibronectin interaction was dependent on FAP binding to fibronectin; however, no role for FAP in the attachment of BCG in vivo has been characterized. We now report the cloning of the M. bovis BCG FAP (FAP-B) and demonstrate an important role for FAP in the in vivo attachment of BCG to the bladder wall and in the induction of BCG-mediated antitumor activity. The predicted amino acid sequence for FAP-B shows 61% and 71% homology, respectively, with Mycobacterium avium FAP (FAP-A) and Mycobacterium leprae FAP (FAP-L). Rabbit polyclonal antibodies against Mycobacterium vaccae FAP (FAP-V) reacted with all 3 recombinant FAP proteins on Western blots. Functional studies show FAP-B to bind fibronectin via the highly conserved attachment regions previously identified for FAP-A and FAP-L and also to competitively inhibit attachment of BCG to matrix fibronectin. In vivo studies show FAP to be a necessary protein for the stable attachment of BCG to the bladder wall. Moreover, stable binding of BCG via FAP was shown to be necessary for the expression of BCG-induced antitumor activity. Our results demonstrate a biological role for FAP in the mediation of BCG-induced antitumor activity.


Asunto(s)
Adhesinas Bacterianas/genética , Vacuna BCG/farmacología , Vacunas contra el Cáncer/farmacología , Mycobacterium bovis/metabolismo , Adhesinas Bacterianas/metabolismo , Secuencia de Aminoácidos , Animales , Vacuna BCG/genética , Adhesión Bacteriana , Secuencia de Bases , Vacunas contra el Cáncer/genética , Clonación Molecular , Fibronectinas/metabolismo , Ratones , Ratones Endogámicos C57BL , Datos de Secuencia Molecular , Mycobacterium bovis/genética , Homología de Secuencia de Aminoácido , Vejiga Urinaria/metabolismo , Neoplasias de la Vejiga Urinaria/terapia
14.
J Biol Chem ; 274(8): 4521-6, 1999 Feb 19.
Artículo en Inglés | MEDLINE | ID: mdl-9988684

RESUMEN

Studies were performed to define the fibronectin binding motif of the previously identified Mycobacterium avium fibronectin attachment protein (FAP-A). Using synthetic peptides of a previously identified fibronectin binding region (amino acids 269-292), the minimal binding sequence was determined to be 12 amino acids, 269-280 (FAP-A-(269-280)). Synthetic peptides were prepared in which each amino acid in the 269-280 sequence was substituted with Ala. Assessment of the effect of Ala substitution on fibronectin binding showed that the presence of Ala at amino acids 273-276 (RWFV) completely abrogated fibronectin binding activity. Furthermore, the ability to inhibit the attachment of viable Mycobacterium bovis BCG to fibronectin was abrogated by Ala substitution at the RWFV sites. To validate the function of RWFV, further studies were performed with recombinant FAP-A in which single Ala mutations were generated for the RWFV sites and as controls at amino acids 269 and 280. Mutant FAP-A containing single Ala substitutions at the RWFV sites (amino acids 273, 274, 275, or 276) showed significant abrogation of fibronectin binding function. Recombinant FAP-A with Ala substitutions at either 269 or 280 showed wild type activity. When the four essential amino acids (RWFV) were either substituted en bloc with Ala or were all deleted, complete loss of fibronectin binding function was observed. Control recombinant proteins with en bloc Ala substitutions or deletions at four positions outside the fibronectin binding region (amino acids 255-257) retained functional activity. These data show that the RWFV sequence is necessary for fibronectin binding function of FAP-A. Furthermore, the data suggest that mycobacterial FAP proteins, all of which share the RWFV binding motif, constitute a family of highly homologous proteins that bind fibronectin in a unique manner.


Asunto(s)
Adhesinas Bacterianas/metabolismo , Fibronectinas/metabolismo , Mycobacterium/metabolismo , Adhesinas Bacterianas/química , Adhesinas Bacterianas/genética , Secuencia de Aminoácidos , Sitios de Unión , Datos de Secuencia Molecular , Mutagénesis Sitio-Dirigida , Homología de Secuencia de Aminoácido
15.
Infect Immun ; 63(7): 2652-7, 1995 Jul.
Artículo en Inglés | MEDLINE | ID: mdl-7790081

RESUMEN

Mycobacterium leprae, the causative agent of leprosy, is an obligate intracellular pathogen. M. leprae can infect a variety of cells in vivo, including epithelial cells, muscle cells, and Schwann cells, in addition to macrophages. The ligand-receptor interactions important in the attachment and ingestion of M. leprae by these nonmacrophage cells remains unknown. Fibronectin (FN) significantly enhances both attachment and ingestion of M. leprae by epithelial and Schwann cell lines. We cloned an M. leprae FN binding protein (FN attachment protein [FAP]) distinct from the 85ABC complex which has been shown previously to bind FN. The FAP open reading frame predicts a protein of 29.5 kDa with a 39-amino-acid signal peptide and was previously described as an antigen in leprosy patients. M. leprae FAP has homologies in M. vaccae, M. avium, and M. tuberculosis, as determined by Southern blotting and direct peptide analysis. Both anti-FAP antibodies and an Escherichia coli-expressed recombinant protein significantly blocked M. leprae attachment and internalization by T-24, an epithelial cell line, and JS1, a Schwann cell line. These data suggest that FN can be a bridging opsonic ligand for attachment of mycobacteria to nonphagocytes and that FAP plays an important role in this process. This may be an important step in the initiation of M. leprae infection in vivo.


Asunto(s)
Adhesinas Bacterianas/genética , Antígenos Bacterianos/genética , Adhesión Bacteriana , Proteínas Bacterianas/genética , Fibronectinas/metabolismo , Genes Bacterianos , Mycobacterium leprae/patogenicidad , Adhesinas Bacterianas/metabolismo , Secuencia de Aminoácidos , Secuencia de Bases , Clonación Molecular , Epitelio/microbiología , Expresión Génica , Datos de Secuencia Molecular , Mycobacterium leprae/genética , Sondas de Oligonucleótidos/química , ARN Mensajero/genética , Células de Schwann/microbiología , Alineación de Secuencia , Homología de Secuencia de Aminoácido
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