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1.
J Microbiol Methods ; 127: 13-19, 2016 08.
Artículo en Inglés | MEDLINE | ID: mdl-27208664

RESUMEN

Two separate species of Ureaplasma have been identified that infect humans: Ureaplasma parvum and Ureaplasma urealyticum. Most notably, these bacteria lack a cell wall and are the leading infectious organism associated with infection-related induction of preterm birth. Fourteen separate representative prototype bacterial strains, called serovars, are largely differentiated by the sequence of repeating units in the C-terminus of the major surface protein: multiple-banded antigen (MBA). Monoclonal antibodies that recognise single or small groups of serovars have been previously reported, but these reagents remain sequestered in individual research laboratories. Here we characterise a panel of commercially available monoclonal antibodies raised against the MBA and describe the first monoclonal antibody that cross-reacts by immunoblot with all serovars of U. parvum and U. urealyticum species. We also describe a recombinant MBA expressed by Escherichia coli which facilitated further characterisation by immunoblot and demonstrate immunohistochemistry of paraffin-embedded antigens. Immunoblot reactivity was validated against well characterised previously published monoclonal antibodies and individual commercial antibodies were found to recognise all U. parvum strains, only serovars 3 and 14 or only serovars 1 and 6, or all strains belonging to U. parvum and U. urealyticum. MBA mass was highly variable between strains, consistent with variation in the number of C-terminal repeats between strains. Antibody characterisation will enable future investigations to correlate severity of pathogenicity to MBA isoform number or mass, in addition to development of antibody-based diagnostics that will detect infection by all Ureaplasma species or alternately be able to differentiate between U. parvum, U. urealyticum or mixed infections.


Asunto(s)
Anticuerpos Antibacterianos/inmunología , Anticuerpos Monoclonales/inmunología , Antígenos Bacterianos/inmunología , Técnicas Inmunológicas , Ureaplasma urealyticum/inmunología , Ureaplasma/inmunología , Anticuerpos Antibacterianos/aislamiento & purificación , Anticuerpos Monoclonales/aislamiento & purificación , Antígenos Bacterianos/genética , Proteínas Bacterianas/genética , ADN Bacteriano , Escherichia coli/genética , Humanos , Immunoblotting , Reacción en Cadena de la Polimerasa , Isoformas de Proteínas/inmunología , Análisis de Secuencia de ADN , Serogrupo , Infecciones por Ureaplasma/diagnóstico , Infecciones por Ureaplasma/inmunología , Infecciones por Ureaplasma/microbiología
2.
Angew Chem Int Ed Engl ; 54(37): 10953-7, 2015 Sep 07.
Artículo en Inglés | MEDLINE | ID: mdl-26216389

RESUMEN

All Enterobacteriaceae express a polysaccharide known as enterobacterial common antigen (ECA), which is an attractive target for the development of universally acting immunotherapies. The first chemical synthesis of ECA-derived oligosaccharides for the development of such therapies is described. A number of synthetic challenges had to be addressed, including the development of concise synthetic procedures for unusual monosaccharides, the selection of appropriate orthogonal protecting groups, the development of stereoselective glycosylation methods, appropriate timing for the introduction of the carboxylic acid groups on the ManpNAcA moieties, and the selection of appropriate conditions for the reduction of multiple azido moieties. The synthetic compounds were employed to uncover immunodominant moieties of ECA. Furthermore, a monoclonal antibody (mAb) was developed that binds to ECA and can selectively recognize a wide range of Enterobacteriaceae species.


Asunto(s)
Antígenos Bacterianos/inmunología , Farmacorresistencia Bacteriana , Inmunoterapia , Enterobacteriaceae/efectos de los fármacos
3.
Virology ; 336(1): 70-82, 2005 May 25.
Artículo en Inglés | MEDLINE | ID: mdl-15866072

RESUMEN

We produced nine monoclonal antibodies (MAbs) directed against the West Nile virus E glycoprotein using three different immunization strategies: inactivated virus, naked DNA, and recombinant protein. Most of the MAbs bound to conformation dependent epitopes in domain III of the E protein. Four of the MAbs neutralized WNV infection and bound to the same region of domain III with high affinity. The neutralizing MAbs were obtained from mice immunized with inactivated virus alone or in combination with a DNA plasmid. In contrast, MAbs obtained by immunization with a soluble version of the E glycoprotein did not exhibit neutralizing activity. These non-neutralizing antibodies were cross-reactive with several other flaviviruses, including Saint Louis encephalitis, Japanese encephalitis, Yellow Fever and Powassan viruses. Interestingly, some non-neutralizing MAbs bound with high affinity to domains I or III, indicating that both affinity and the precise epitope recognized by an antibody are important determinants of WNV neutralization.


Asunto(s)
Anticuerpos Monoclonales/inmunología , Anticuerpos Antivirales/inmunología , Virus del Nilo Occidental/inmunología , Animales , Antígenos Virales/inmunología , Reacciones Cruzadas , Virus de la Encefalitis Japonesa (Especie)/inmunología , Virus de la Encefalitis de San Luis/inmunología , Virus de la Encefalitis Transmitidos por Garrapatas/inmunología , Ensayo de Inmunoadsorción Enzimática , Mapeo Epitopo , Epítopos/inmunología , Glicoproteínas/inmunología , Ratones , Pruebas de Neutralización , Estructura Terciaria de Proteína , Virus de la Fiebre Amarilla/inmunología
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