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1.
Clin Neurol Neurosurg ; 221: 107381, 2022 10.
Artigo em Inglês | MEDLINE | ID: mdl-35901556

RESUMO

OBJECTIVE: Optic neuritis (ON) is an immune-mediated optic neuropathy associated with multiple immune-mediated neurological conditions. Our aim was to characterize the clinical and diagnostic features of first or initial episodes of ON associated with multiple sclerosis (MS)-associated (typical) and antibody-related (atypical) ON. METHODS: Retrospective, single institution, medical record review. We analyzed demographic, clinical, laboratory, and radiographic findings of 139 patients who presented with first episodes of MS-associated ON (MS-ON), aquaporin 4 antibody-associated ON (AQP4-ON), and myelin oligodendrocyte glycoprotein antibody-associated ON (MOG-ON) between January 2015 and October 2019 without preceding diagnosis. Simple hypothesis testing assessed differences between groups were performed. RESULTS: Of 139 patients (109 [79 %] women; 29 [21 %] men; mean age 47 [SD, 14] years), 106 had MS-ON, 25 had AQP4-ON, and 8 had MOG-ON. Patients with MOG-ON had the highest recurrence rate (88 %) relative to MS-ON (28 %) and AQP4-ON (56 %) patients (P < .001). Patients with AQP4-ON had the highest mean visual functional system scores (4.3 [SD, 1.8]) relative to MS-ON (2.0 [SD, 1.9]) and MOG-ON patients (2.8 [SD, 2.0]) (P < .001). CONCLUSION: Patients presenting with initial episodes of ON exhibit a range radiographic and laboratory feature depending on the underlying associated disease. Understanding the variable characteristics of typical (MS-associated) and atypical (antibody-associated) ON may help physicians accurately diagnose and effectively treat ON.


Assuntos
Esclerose Múltipla , Neurite Óptica , Aquaporina 4 , Autoanticorpos , Feminino , Humanos , Masculino , Esclerose Múltipla/diagnóstico , Esclerose Múltipla/diagnóstico por imagem , Glicoproteína Mielina-Oligodendrócito , Oligodendroglia , Neurite Óptica/diagnóstico , Estudos Retrospectivos
2.
J Proteins Proteom ; 12(3): 177-184, 2021.
Artigo em Inglês | MEDLINE | ID: mdl-34456530

RESUMO

Outbreak of COVID-19 by SARS-CoV-2 infection caused severe acute respiratory syndrome that has been declared a public health emergency of international concern. To control infections, there is urgent need to develop an effective therapeutic strategy. COVID-19 viral spike glycoprotein and proteases play major role in viral entry and mediating virus replication and spread and thus can serve as potential antiviral drug target. Being highly specific, efficacious and safe, peptides hold their place in therapeutics. In present study, molecular docking of 21 pharmacologically active non ribosomal peptides (NRPs) from marine microbes with SARS-CoV-2 spike glycoprotein and papain such as protease was done. Dactinomycin, Tyrocidine A and Gramicidin S showed highest binding interaction with target proteins. The binding affinity of Dactinomycin and Gramicidin S docked with SARS-CoV-2 spike glycoprotein was - 12.4 kcal/mol and - 11.4 kcal/mol, respectively. This suggested their potential to destabilize SARS spike protein binding with human host ACE2 receptor and thus hindering viral entry to the cells. Binding affinity of Tyrocidine A and Gramicidin S with SARS-CoV-2 papain-like protease was - 13.1 kcal/mol and - 11.4 kcal/mol, respectively which might be inhibited COVID-19 by acting on the protease. Gramicidin S showed same binding affinity for both target proteins and thus expected to be most potent. Based on the binding energy score, it was suggested that these pharmacologically active NRPs are potential molecules to be tested against SARS-CoV-2 and used to develop effective antiviral drugs.

4.
World J Microbiol Biotechnol ; 36(1): 10, 2019 Dec 20.
Artigo em Inglês | MEDLINE | ID: mdl-31863307

RESUMO

Aggregation and adhesion capability and survival efficacy of candidate probiotic strain Pediococcus acidilactici NCDC 252 under simulated gastric, intestinal and vaginal conditions was studied. The strain exhibited strong autoaggregation phenotype and coaggregation with other Lactic acid bacteria (LAB) and E. coli. The adhesion studies of NCDC 252 to pig's intestinal epithelial cells showed its adhesive ability. Aggregation and adhesiveness were related through cell surface proteins as removal/extraction of surface proteins resulted in altered aggregation and no adhesiveness. Cell surface proteins were analysed by SDS-PAGE and also in silico analysed from its genome. SDS-PAGE analysis of cell surface proteins of NCDC 252 revealed two potential proteins of approximately 74.3 and 53.6 kDa to be involved in host-probiotic interaction. Removal of cell surface proteins by LiCl-treatment (5 mol l-1) resulted in loss of aggregation and adhesiveness. Further survival of NCDC 252 under simulated gastrointestinal and vaginal conditions in terms of high viable counts confirmed its efficacy for its survival under gut and urogenital conditions. These observations suggest that it can be used further in functional foods, nutraceuticals and in combating urogenital infections. As NCDC 252 was able to survive in intestinal conditions, interaction of its cell surface proteins with intestinal mucins was studied in silico by docking. Highest affinity of adhesion was observed for MUC3B. In conclucion, NCDC 252, exhibited aggregation phenotype and adhesion capability. Survivability of NCDC 252 under simulated conditions and its interaction with human mucins confirms its efficacy to be used as probiotic.


Assuntos
Aderência Bacteriana/fisiologia , Pediococcus acidilactici/fisiologia , Probióticos/metabolismo , Animais , Suplementos Nutricionais , Células Epiteliais/microbiologia , Feminino , Trato Gastrointestinal/microbiologia , Humanos , Lactobacillales/fisiologia , Proteínas de Membrana , Viabilidade Microbiana , Simulação de Acoplamento Molecular , Mucinas , Vagina/microbiologia
5.
Mol Biol Rep ; 46(6): 5883-5895, 2019 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-31392538

RESUMO

Pediococcus acidilactici NCDC 252 is a facultative anaerobe of dairy origin that possessed all studied in vitro probiotic attributes and several useful enzyme activities. Its whole genome was sequenced and analysed for its evolutionary relationship with other lactic acid bacteria (LAB). This is a novel sequence and first report of genome sequence of P. acidilactici of dairy origin. Its genome is relatively larger than other studied genomes of P. acidilactici and is comprised of 40 scaffolds that totals to 3,243,337 bases and 44.5% GC content. A total of 3054 coding sequences (CDS) were identified by RAST and DIAMOND servers. The genome also encoded different enzyme activities required for utilization of various carbohydrates. This was also confirmed by carbohydrate utilization studies. The genome also encoded genes for probiotics properties. The phylogenetic analysis of P. acidilactici NCDC 252 genome was done using Maximum Parsimony and Maximum Likelihood methods to study its evolution and relatedness to other LABs based upon their 16S rDNA sequences. The strain exhibited highest resemblance to Lactobacillus plantarum WCFS1 and is also much close to P. acidilactici based on similarity of ribosomal protein. The strain seems to have acquired some genes for its adaptation in dairy/environmental niche. This genome sequence is novel with genome more similar to L. plantarum and biochemical and phenotypic characteristics of P. acidilactici.


Assuntos
Pediococcus acidilactici/enzimologia , Pediococcus acidilactici/genética , Pediococcus acidilactici/metabolismo , Evolução Biológica , DNA Ribossômico , Evolução Molecular , Sequenciamento de Nucleotídeos em Larga Escala/métodos , Ácido Láctico/metabolismo , Lactobacillales/genética , Lactobacillales/metabolismo , Redes e Vias Metabólicas , Pediococcus/genética , Filogenia , Probióticos
6.
Neurohospitalist ; 6(2): 87-8, 2016 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-27053987
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