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1.
Laryngoscope Investig Otolaryngol ; 9(1): e1205, 2024 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-38362199

RESUMO

Objective: To assess the extent of recurrent laryngeal nerve (RLN) and superior laryngeal nerve (SLN) damage in patients with idiopathic vocal cord paralysis (IVCP) exhibiting different paralytic sides. Methods: A total of 84 IVCP cases were evaluated using stroboscopic laryngoscopy, voice analysis, and laryngeal electromyography (LEMG). The results were compared between patients with left-sided paralysis and right-sided paralysis based on different disease courses (less than or more than 3 months). Results: Initially, the average age and disease progression of IVCP patients were found to be similar regardless of the side of paralysis (p > .05). Additionally, there were no significant variations in voice indicators, such as MPT, DSI, and VHI, between IVCP patients with left and right vocal cord paralysis (p > .05). Furthermore, no disparities were detected in the latencies and amplitudes of the paralyzed RLN and SLN, as well as the durations and amplitudes of the action potentials in the paralyzed TM and PCM, among IVCP patients with left and right vocal cord paralysis (p > .05). Notably, the amplitudes of the left paralytic CM were significantly lower than those of the right paralytic CM (0.45 vs. 0.53, Z = -2.013, p = .044). In addition, no disparities were observed in APDs and amplitudes between the ipsilateral PCM and TM, either for patients with left or right vocal fold paralysis (p > .05). Finally, all the IVCP patients were subdivided into two subgroups according to different disease course (less than or more than 3 months), and in each subgroup, the comparison of voice indicators and LEMG results in IVCP patients with left or right vocal fold paralysis were similar with the above findings (p > .05). Conclusion: Overall, the degree of RLN and SLN damage appeared to be similar in IVCP patients with left and right vocal cord paralysis, provided that the disease course was comparable. Level of Evidence: 4.

2.
J Hazard Mater ; 433: 128816, 2022 07 05.
Artigo em Inglês | MEDLINE | ID: mdl-35390614

RESUMO

Poly (ethylene terephthalate) (PET) is a widely used type of general plastic that produces a significant amount of waste due to its non-degradable properties. We propose a novel directional-path modification (DPM) strategy, involving positive charge amino acid introduction and binding groove remodeling, and apply it to Thermobifida fusca cutinase to enhance PET degradation. The highest value of PET degradation (90%) was achieved in variant 4Mz (H184S/Q92G/F209I/I213K), exhibiting values almost 30-fold that of the wild-type. We employed molecular docking, molecular dynamics simulations, and QM/MM MD for the degradation process of PET, accompanied by acylation and deacylation. We found that the distance of nucleophilic attack was reduced from about 4.6 Å in the wild type to 3.8 Å in 4Mz, and the free energy barrier of 4Mz dropped from 14.3 kcal/mol to 7.1 kcal/mol at the acylation which was the rate-limiting step. Subsequently, the high efficiency and universality of the DPM strategy were successfully demonstrated in LCC, Est119, and BhrPETase enhancing the degradation activity of PET. Finally, the highest degradation rate of the pretreated commercial plastic bottles had reached to 73%. The present study provides insight into the molecular binding mechanism of PET into the PET hydrolases structure and proposes a novel DPM strategy that will be useful for the engineering of more efficient enzymes for PET degradation.


Assuntos
Hidrolases , Plásticos , Catálise , Hidrolases/metabolismo , Simulação de Acoplamento Molecular , Polietilenotereftalatos/química , Polietilenotereftalatos/metabolismo
3.
Dev Comp Immunol ; 117: 103981, 2021 04.
Artigo em Inglês | MEDLINE | ID: mdl-33340592

RESUMO

Peritrophic membrane (PM) refers to a vital physical barrier enabling shrimp to resist pathogen invasion. It primarily consists of chitin and proteins, mostly chitin-binding protein (CBP). CBPs have been identified from microorganisms to higher organisms. In the present study, a CBP, designated MjCBP, was reported from Marsupenaeus japonicus. The open reading frame of MjCBP was 1854 bp, encoding a protein with 618 amino acids (MH544098). To be specific, the theoretical pI and molecular mass of mature MjCBP reached 5.43 and 66064.00 Da, respectively. MjCBP consisted of seven type Ⅱ chitin-binding domains (ChtB D2), which was up-regulated after being challenged with Vibrio anguillarum and then agglutinating several bacteria. In addition, MjCBP and the first chitin-binding domain (CBD1) could bind to several Gram-positive and Gram-negative bacteria via the binding process to lipopolysaccharides and peptidoglycans, whereas CBD1 was not capable of agglutinating bacteria. Moreover, the anterior and posterior segments of CBD1 were synthesized in vitro, and the posterior segment could bind to lipopolysaccharides. However, both segments fail to agglutinate bacteria. Furthermore, MjCBP and CBD1 facilitated the clearance of V. anguillarum in vivo, and the silencing of MjCBP via RNA interference reduced the ability of bacterial clearance. As revealed from the mentioned results, MjCBP acts as an opsonin or pattern recognition receptor to achieve antibacterial immune response in shrimp.


Assuntos
Proteínas de Artrópodes/imunologia , Proteínas de Transporte/imunologia , Quitina/metabolismo , Imunidade Inata/imunologia , Penaeidae/imunologia , Vibrio/imunologia , Sequência de Aminoácidos , Animais , Proteínas de Artrópodes/genética , Proteínas de Artrópodes/metabolismo , Proteínas de Transporte/classificação , Proteínas de Transporte/genética , Perfilação da Expressão Gênica/métodos , Hemócitos/imunologia , Hemócitos/metabolismo , Hemócitos/microbiologia , Interações Hospedeiro-Patógeno/imunologia , Imunidade Inata/genética , Penaeidae/genética , Penaeidae/microbiologia , Ligação Proteica , Interferência de RNA , Homologia de Sequência de Aminoácidos , Vibrio/metabolismo , Vibrio/fisiologia
4.
Fish Shellfish Immunol ; 98: 354-363, 2020 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-31945483

RESUMO

L-type lectins (LTLs) belong to the lectin family and are characterized by a conserved structural motif in their carbohydrate recognition domain. LTLs are homologous to leguminous lectins. In this study, we identified and functionally characterized an LTL from kuruma shrimp Marsupenaeus japonicus. We designated this LTL as MjLTL2. MjLTL2 contains a signal peptide, a Lectin_leg domain, a coiled coil, and transmembrane domain. MjLTL2 is distributed in hemocytes, heart, hepatopancreas, gill, stomach, and intestine; higher expression levels are seen in hemocytes and the hepatopancreas than in other tissues. MjLTL2 was upregulated following challenge of shrimp with Vibrio anguillarum and white spot syndrome virus (WSSV). MjLTL2 can agglutinate several bacteria without Ca2+. In addition, MjLTL2 could bind to several Gram-positive and -negative bacteria by binding to their lipopolysaccharide and peptidoglycan. However, MjLTL2 could not enhance the clearance of V. anguillarum in vivo. In the presence of WSSV infection, MjLTL2 knockdown by RNA interference resulted in a 7-day lower cumulative mortality of M. japonicus. Moreover, less VP19, VP24, VP26, and VP28 mRNAs were extracted from the hemocytes of MjLTL2 knockdown shrimp than from the control. These results suggest that MjLTL2 is involved in immune responses in shrimp.


Assuntos
Proteínas de Artrópodes/metabolismo , Lectinas/metabolismo , Penaeidae/imunologia , Testes de Aglutinação , Sequência de Aminoácidos , Animais , Proteínas de Artrópodes/química , Proteínas de Artrópodes/genética , Resistência à Doença/genética , Regulação da Expressão Gênica , Imunidade Inata , Lectinas/química , Lectinas/genética , Penaeidae/classificação , Penaeidae/genética , Filogenia , Polissacarídeos Bacterianos/metabolismo , Alinhamento de Sequência , Taxa de Sobrevida , Distribuição Tecidual , Vibrio/fisiologia , Replicação Viral , Vírus da Síndrome da Mancha Branca 1/fisiologia
5.
Mitochondrial DNA B Resour ; 4(2): 3523-3524, 2019 Oct 11.
Artigo em Inglês | MEDLINE | ID: mdl-33366068

RESUMO

Pholidota imbricata belongs to tribe Coelogninae in Orchidaceae distributed in Sichuan, Xizang, and Yunnan. Here, we report the first complete chloroplast (cp) genome and the cp genome features of P. imbricata. The complete cp genome sequence of P. imbricata is 159,292 bp in length and presented a typical quadripartite structure including one large single-copy region (LSC, 87,515 bp), one small single-copy region (SSC, 20,999 bp), and two inverted repeat regions (IRs, 25,389 bp each). The cp genome encoded 141 genes, of which 108 were unique genes (80 protein-coding genes, 24 tRNAs, and 4 rRNAs). The phylogenetic relationships show that P. imbricata is sister to the species of the genus Pleione in tribe Coelogninae.

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