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1.
BMC Bioinformatics ; 25(1): 282, 2024 Aug 28.
Artigo em Inglês | MEDLINE | ID: mdl-39198740

RESUMO

BACKGROUND: Thermostability is a fundamental property of proteins to maintain their biological functions. Predicting protein stability changes upon mutation is important for our understanding protein structure-function relationship, and is also of great interest in protein engineering and pharmaceutical design. RESULTS: Here we present mutDDG-SSM, a deep learning-based framework that uses the geometric representations encoded in protein structure to predict the mutation-induced protein stability changes. mutDDG-SSM consists of two parts: a graph attention network-based protein structural feature extractor that is trained with a self-supervised learning scheme using large-scale high-resolution protein structures, and an eXtreme Gradient Boosting model-based stability change predictor with an advantage of alleviating overfitting problem. The performance of mutDDG-SSM was tested on several widely-used independent datasets. Then, myoglobin and p53 were used as case studies to illustrate the effectiveness of the model in predicting protein stability changes upon mutations. Our results show that mutDDG-SSM achieved high performance in estimating the effects of mutations on protein stability. In addition, mutDDG-SSM exhibited good unbiasedness, where the prediction accuracy on the inverse mutations is as well as that on the direct mutations. CONCLUSION: Meaningful features can be extracted from our pre-trained model to build downstream tasks and our model may serve as a valuable tool for protein engineering and drug design.


Assuntos
Mutação , Estabilidade Proteica , Proteínas , Proteínas/química , Proteínas/genética , Proteínas/metabolismo , Mioglobina/química , Mioglobina/genética , Proteína Supressora de Tumor p53/genética , Proteína Supressora de Tumor p53/química , Proteína Supressora de Tumor p53/metabolismo , Biologia Computacional/métodos , Aprendizado Profundo , Aprendizado de Máquina Supervisionado , Bases de Dados de Proteínas , Conformação Proteica
2.
J Virol ; 97(10): e0093823, 2023 10 31.
Artigo em Inglês | MEDLINE | ID: mdl-37792003

RESUMO

IMPORTANCE: Human norovirus (HuNoV) is highly infectious and can result in severe illnesses in the elderly and children. So far, there is no effective antiviral drug to treat HuNoV infection, and thus, the development of HuNoV vaccines is urgent. However, NoV evolves rapidly, and currently, at least 10 genogroups with numerous genotypes have been found. The genetic diversity of NoV and the lack of cross-protection between different genotypes pose challenges to the development of broadly protective vaccines. In this study, guided by structural alignment between GI.1 and GII.4 HuNoV VP1 proteins, several chimeric-type virus-like particles (VLPs) were designed through surface-exposed loop grafting. Mouse immunization studies show that two of the designed chimeric VLPs induced cross-immunity against both GI.1 and GII.4 HuNoVs. To our knowledge, this is the first designed chimeric VLPs that can induce cross-immune activities across different genogroups of HuNoV, which provides valuable strategies for the development of cross-reactive HuNoV vaccines.


Assuntos
Infecções por Caliciviridae , Epitopos , Genótipo , Norovirus , Vacinas Virais , Vírion , Animais , Humanos , Camundongos , Infecções por Caliciviridae/imunologia , Infecções por Caliciviridae/prevenção & controle , Infecções por Caliciviridae/virologia , Epitopos/química , Epitopos/genética , Epitopos/imunologia , Imunização , Norovirus/química , Norovirus/classificação , Norovirus/genética , Norovirus/imunologia , Vacinas Virais/química , Vacinas Virais/genética , Vacinas Virais/imunologia , Quimera/genética , Quimera/imunologia , Proteínas do Capsídeo/química , Proteínas do Capsídeo/genética , Proteínas do Capsídeo/imunologia , Vírion/química , Vírion/genética , Vírion/imunologia
3.
PLoS Pathog ; 17(7): e1009745, 2021 07.
Artigo em Inglês | MEDLINE | ID: mdl-34252166

RESUMO

Norovirus (NoV) is the major pathogen causing the outbreaks of the viral gastroenteritis across the world. Among the various genotypes of NoV, GII.4 is the most predominant over the past decades. GII.4 NoVs interact with the histo-blood group antigens (HBGAs) to invade the host cell, and it is believed that the receptor HBGAs may play important roles in selecting the predominate variants by the nature during the evolution of GII.4 NoVs. However, the evolution-induced changes in the HBGA-binding affinity for the GII.4 NoV variants and the mechanism behind the evolution of the NoV-HBGA interactions remain elusive. In the present work, the virus-like particles (VLPs) of the representative GII.4 NoV stains epidemic in the past decades were expressed by using the Hansenula polymorpha yeast expression platform constructed by our laboratory, and then the enzyme linked immunosorbent assay (ELISA)-based HBGA-binding assays as well as the molecular dynamics (MD) simulations combined with the molecular mechanics/generalized born surface area (MMGBSA) calculations were performed to investigate the interactions between various GII.4 strains and different types of HBGAs. The HBGA-binding assays show that for all the studied types of HBGAs, the evolution of GII.4 NoVs results in the increased NoV-HBGA binding affinities, where the early epidemic strains have the lower binding activity and the newly epidemic strains exhibit relative stronger binding intensity. Based on the MD simulation and MMGBSA calculation results, a physical mechanism that accounts for the increased HBGA-binding affinity was proposed. The evolution-involved residue mutations cause the conformational rearrangements of loop-2 (residues 390-396), which result in the narrowing of the receptor-binding pocket and thus tighten the binding of the receptor HBGAs. Our experimental and computational studies are helpful for better understanding the mechanism behind the evolution-induced increasing of HBGA-binding affinity, which may provide useful information for the drug and vaccine designs against GII.4 NoVs.


Assuntos
Antígenos de Grupos Sanguíneos/metabolismo , Interações Hospedeiro-Parasita/fisiologia , Norovirus/metabolismo , Humanos , Simulação de Acoplamento Molecular , Norovirus/genética , Ligação Viral
4.
J Nanosci Nanotechnol ; 18(5): 3709-3712, 2018 May 01.
Artigo em Inglês | MEDLINE | ID: mdl-29442888

RESUMO

CdS nanowires arrays were successfully synthesized by a simple solvothermal process using AAO as templates. The phase structures, morphologies, and optical properties of the products were investigated by X-ray diffraction, scanning electron microscopy, high-resolution transmission electron microscopy, Raman spectroscopy, and photoluminescence spectroscopy. It was found that the nanowires were composed of hexagonal structure CdS nanoparticles and the average diameters is about 60-70 nm. A strong green emission with a maximum around 505 nm was observed from the synthesized CdS nanowires at room temperature, which was attributed to near-band-edge emission. A 3D self-seed nucleation coalescent process was proposed for the formation of CdS nanowires structures. The present synthetic route is expected to be applied to the synthesis of other II-VI groups or other group's 1D semiconducting materials.

5.
Science ; 385(6716): 1484-1491, 2024 Sep 27.
Artigo em Inglês | MEDLINE | ID: mdl-39325881

RESUMO

The respiratory syncytial virus (RSV) fusion (F) glycoprotein is highly immunogenic in its prefusion (pre-F) conformation. However, the protein is unstable, and its conformation must be stabilized for it to function effectively as an immunogen in vaccines. We present a mutagenesis strategy to arrest the RSV F protein in its pre-F state by blocking localized changes in protein structure that accompany large-scale conformational rearrangements. We generated a series of mutants and screened them in vitro to assess their potential for forming a stable pre-F. In animals, the immunogenicity of a representative mutant F protein, with a conformation confirmed by cryo-electron microscopy, elicited levels of neutralizing antibodies and protection against RSV-induced lung damage that were comparable to those of DS-Cav1, a pre-F used in a licensed vaccine.


Assuntos
Infecções por Vírus Respiratório Sincicial , Vacinas contra Vírus Sincicial Respiratório , Vírus Sincicial Respiratório Humano , Proteínas Virais de Fusão , Animais , Humanos , Camundongos , Anticorpos Neutralizantes/imunologia , Anticorpos Antivirais/imunologia , Microscopia Crioeletrônica , Imunogenicidade da Vacina , Pulmão/virologia , Camundongos Endogâmicos BALB C , Mutagênese , Mutação , Conformação Proteica , Estabilidade Proteica , Infecções por Vírus Respiratório Sincicial/imunologia , Infecções por Vírus Respiratório Sincicial/prevenção & controle , Vacinas contra Vírus Sincicial Respiratório/imunologia , Vacinas contra Vírus Sincicial Respiratório/química , Vacinas contra Vírus Sincicial Respiratório/genética , Vírus Sincicial Respiratório Humano/genética , Vírus Sincicial Respiratório Humano/imunologia , Proteínas Virais de Fusão/química , Proteínas Virais de Fusão/imunologia , Proteínas Virais de Fusão/genética
6.
NPJ Vaccines ; 9(1): 62, 2024 Mar 19.
Artigo em Inglês | MEDLINE | ID: mdl-38503757

RESUMO

Respiratory syncytial virus (RSV) is one of the most important pathogens causing respiratory tract infection in humans, especially in infants and the elderly. The identification and structural resolution of the potent neutralizing epitopes on RSV fusion (F) protein enable an "epitope-focused" vaccine design. However, the display of RSV F epitope II on the surface of the widely-used human hepatitis B virus core antigen (HBcAg) has failed to induce neutralizing antibody response in mice. Here, we used the hepadnavirus core protein (HcAg) from different mammalian hosts as scaffolds to construct chimeric virus-like particles (VLPs) presenting the RSV F epitope II. Mouse immunization showed that different HcAg-based chimeric VLPs elicited significantly different neutralizing antibody responses, among which the HcAg derived from roundleaf bat (RBHcAg) is the most immunogenic. Furthermore, RBHcAg was used as the scaffold platform to present multiple RSV F epitopes, and the immunogenicity was further improved in comparison to that displaying a single epitope II. The designed RBHcAg-based multiple-epitope-presenting VLP formulated with MF59-like adjuvant elicited a potent and balanced Th1/Th2 immune response, and offered substantial protection in mice against the challenge of live RSV A2 virus. The designed chimeric VLPs may serve as the potential starting point for developing epitope-focused vaccines against RSV. Our study also demonstrated that RBHcAg is an effective VLP carrier for presenting foreign epitopes, providing a promising platform for epitope-focused vaccine design.

7.
J Virol ; 86(21): 11953, 2012 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-23043181

RESUMO

Here, we report three complete genome sequences of porcine torque teno virus type I (TTV1) which were obtained from swine tissues and sera from southern China through routine and nested PCR amplification and characterized together with other genome sequences already deposited in GenBank. The results showed that the TTV1 sequences were highly divergent and could be divided into 1a and 1b subtypes.


Assuntos
DNA Viral/química , DNA Viral/genética , Genoma Viral , Torque teno virus/genética , Animais , China , Genótipo , Dados de Sequência Molecular , Filogenia , Análise de Sequência de DNA , Suínos , Torque teno virus/classificação , Torque teno virus/isolamento & purificação
8.
J Virol ; 86(22): 12465, 2012 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-23087122

RESUMO

Through routine and nested PCR amplifications, four complete genome sequences of porcine Torque teno virus (TTV) type II were obtained from swine herds. By comparison with the TTV genome sequences deposited in GenBank, we found the most divergent types so far described. The level of genetic diversity between these genomes is higher than would be expected within a single virus species. A nucleotide and amino acid phylogenetic tree was constructed.


Assuntos
Genoma Viral , Torque teno virus/genética , Animais , DNA Viral , Bases de Dados Genéticas , Genes Virais , Variação Genética , Dados de Sequência Molecular , Fases de Leitura Aberta , Filogenia , Suínos
9.
Signal Transduct Target Ther ; 8(1): 20, 2023 01 03.
Artigo em Inglês | MEDLINE | ID: mdl-36596779

RESUMO

An ongoing randomized, double-blind, controlled phase 2 trial was conducted to evaluate the safety and immunogenicity of a mosaic-type recombinant vaccine candidate, named NVSI-06-09, as a booster dose in subjects aged 18 years and older from the United Arab Emirates (UAE), who had administered two or three doses of inactivated vaccine BBIBP-CorV at least 6 months prior to enrollment. The participants were randomly assigned with 1:1 to receive a booster dose of NVSI-06-09 or BBIBP-CorV. The primary outcomes were immunogenicity and safety against severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) Omicron variant, and the exploratory outcome was cross-immunogenicity against other circulating strains. Between May 25 and 30, 2022, 516 adults received booster vaccination with 260 in NVSI-06-09 group and 256 in BBIBP-CorV group. Interim results showed a similar safety profile between two booster groups, with low incidence of adverse reactions of grade 1 or 2. For immunogenicity, by day 14 post-booster, the fold rises in neutralizing antibody geometric mean titers (GMTs) from baseline elicited by NVSI-06-09 were remarkably higher than those by BBIBP-CorV against the prototype strain (19.67 vs 4.47-fold), Omicron BA.1.1 (42.35 vs 3.78-fold), BA.2 (25.09 vs 2.91-fold), BA.4 (22.42 vs 2.69-fold), and BA.5 variants (27.06 vs 4.73-fold). Similarly, the neutralizing GMTs boosted by NVSI-06-09 against Beta and Delta variants were also 6.60-fold and 7.17-fold higher than those by BBIBP-CorV. Our findings indicated that a booster dose of NVSI-06-09 was well-tolerated and elicited broad-spectrum neutralizing responses against divergent SARS-CoV-2 variants, including Omicron and its sub-lineages.


Assuntos
COVID-19 , Vacinas , Adulto , Humanos , SARS-CoV-2 , COVID-19/prevenção & controle
10.
Elife ; 112022 08 25.
Artigo em Inglês | MEDLINE | ID: mdl-36004719

RESUMO

Large-scale populations in the world have been vaccinated with COVID-19 vaccines, however, breakthrough infections of SARS-CoV-2 are still growing rapidly due to the emergence of immune-evasive variants, especially Omicron. It is urgent to develop effective broad-spectrum vaccines to better control the pandemic of these variants. Here, we present a mosaic-type trimeric form of spike receptor-binding domain (mos-tri-RBD) as a broad-spectrum vaccine candidate, which carries the key mutations from Omicron and other circulating variants. Tests in rats showed that the designed mos-tri-RBD, whether used alone or as a booster shot, elicited potent cross-neutralizing antibodies against not only Omicron but also other immune-evasive variants. Neutralizing antibody ID50 titers induced by mos-tri-RBD were substantially higher than those elicited by homo-tri-RBD (containing homologous RBDs from prototype strain) or the BIBP inactivated COVID-19 vaccine (BBIBP-CorV). Our study indicates that mos-tri-RBD is highly immunogenic, which may serve as a broad-spectrum vaccine candidate in combating SARS-CoV-2 variants including Omicron.


The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) pandemic continues to pose a serious threat to public health and has so far resulted in over six million deaths worldwide. Mass vaccination programs have reduced the risk of serious illness and death in many people, but the virus continues to persist and circulate in communities across the globe. Furthermore, the current vaccines may be less effective against the new variants of the virus, such as Omicron and Delta, which are continually emerging and evolving. Therefore, it is urgent to develop effective vaccines that can provide broad protection against existing and future forms of SARS-CoV-2. There are several different types of SARS-CoV-2 vaccine, but they all work in a similar way. They contain molecules that induce immune responses in individuals to help the body recognize and more effectively fight SARS-CoV-2 if they happen to encounter it in the future. These immune responses may be so specific that new variants of a virus may not be recognized by them. Therefore, a commonly used strategy for producing vaccines with broad protection is to make multiple vaccines that each targets different variants and then mix them together before administering to patients. Here, Zhang et al. took a different approach by designing a new vaccine candidate against SARS-CoV2 that contained three different versions of part of a SARS-CoV2 protein ­ the so-called spike protein ­ all linked together as one molecule. The different versions of the spike protein fragment were designed to include key features of the fragments found in Omicron and several other SARS-CoV-2 variants. The experiments found that this candidate vaccine elicited a much higher immune response against Omicron and other SARS-CoV-2 variants in rats than an existing SARS-CoV-2 vaccine. It was also effective as a booster shot after a first vaccination with the existing SARS-CoV-2 vaccine. These findings demonstrate that the molecule developed by Zhang et al. induces potent and broad immune responses against different variants of SARS-CoV-2 including Omicron in rats. The next steps following on from this work are to evaluate the safety and immunogenicity of this vaccine candidate in clinical trials. In the future, it may be possible to use a similar approach to develop new broad-spectrum vaccines against other viruses.


Assuntos
Vacinas contra COVID-19 , COVID-19 , Animais , Anticorpos Neutralizantes , Anticorpos Antivirais , Anticorpos Amplamente Neutralizantes , COVID-19/prevenção & controle , Humanos , Ratos , SARS-CoV-2/genética , Glicoproteína da Espícula de Coronavírus/química
11.
Cell Discov ; 8(1): 17, 2022 Feb 15.
Artigo em Inglês | MEDLINE | ID: mdl-35169113

RESUMO

The continuous emergence of SARS-CoV-2 variants highlights the need of developing vaccines with broad protection. Here, according to the immune-escape capability and evolutionary convergence, the representative SARS-CoV-2 strains carrying the hotspot mutations were selected. Then, guided by structural and computational analyses, we present a mutation-integrated trimeric form of spike receptor-binding domain (mutI-tri-RBD) as a broadly protective vaccine candidate, which combined heterologous RBDs from different representative strains into a hybrid immunogen and integrated immune-escape hotspots into a single antigen. When compared with a homo-tri-RBD vaccine candidate in the stage of phase II trial, of which all three RBDs are derived from the SARS-CoV-2 prototype strain, mutI-tri-RBD induced significantly higher neutralizing antibody titers against the Delta and Beta variants, and maintained a similar immune response against the prototype strain. Pseudo-virus neutralization assay demonstrated that mutI-tri-RBD also induced broadly strong neutralizing activities against all tested 23 SARS-CoV-2 variants. The in vivo protective capability of mutI-tri-RBD was further validated in hACE2-transgenic mice challenged by the live virus, and the results showed that mutI-tri-RBD provided potent protection not only against the SARS-CoV-2 prototype strain but also against the Delta and Beta variants.

12.
Nat Commun ; 13(1): 3654, 2022 06 27.
Artigo em Inglês | MEDLINE | ID: mdl-35760812

RESUMO

NVSI-06-08 is a potential broad-spectrum recombinant COVID-19 vaccine that integrates the antigens from multiple SARS-CoV-2 strains into a single immunogen. Here, we evaluate the safety and immunogenicity of NVSI-06-08 as a heterologous booster dose in BBIBP-CorV recipients in a randomized, double-blind, controlled, phase 2 trial conducted in the United Arab Emirates (NCT05069129). Three groups of healthy adults over 18 years of age (600 participants per group) who have administered two doses of BBIBP-CorV 4-6-month, 7-9-month and >9-month earlier, respectively, are randomized 1:1 to receive either a homologous booster of BBIBP-CorV or a heterologous booster of NVSI-06-08. The incidence of adverse reactions is low, and the overall safety profile is quite similar between two booster regimens. Both Neutralizing and IgG antibodies elicited by NVSI-06-08 booster are significantly higher than those by BBIBP-CorV booster against not only SARS-CoV-2 prototype strain but also multiple variants of concerns (VOCs). Especially, the neutralizing antibody GMT against Omicron variant induced by heterologous NVSI-06-08 booster reaches 367.67, which is substantially greater than that boosted by BBIBP-CorV (GMT: 45.03). In summary, NVSI-06-08 is safe and immunogenic as a booster dose following two doses of BBIBP-CorV, which is immunogenically superior to the homologous boost with another dose of BBIBP-CorV.


Assuntos
Vacinas contra COVID-19 , COVID-19 , Imunização Secundária , Imunogenicidade da Vacina , Adulto , Anticorpos Neutralizantes , Anticorpos Antivirais , COVID-19/prevenção & controle , Vacinas contra COVID-19/efeitos adversos , Vacinas contra COVID-19/imunologia , Humanos , Imunoglobulina G , SARS-CoV-2
13.
Oncogene ; 40(7): 1375-1389, 2021 02.
Artigo em Inglês | MEDLINE | ID: mdl-33420374

RESUMO

Arginine methylation is an important posttranslational modification catalyzed by protein arginine methyltransferases (PRMTs). However, the role of PRMTs in colorectal cancer (CRC) progression is not well understood. Here we report that non-POU domain-containing octamer-binding protein (NONO) is overexpressed in CRC tissue and is a potential marker for poor prognosis in CRC patients. NONO silencing resulted in decreased proliferation, migration, and invasion of CRC cells, whereas overexpression had the opposite effect. In a xenograft model, tumors derived from NONO-deficient CRC cells were smaller than those derived from wild-type (WT) cells, and PRMT1 inhibition blocked CRC xenograft progression. A mass spectrometry analysis indicated that NONO is a substrate of PRMT1. R251 of NONO was asymmetrically dimethylated by PRMT1 in vitro and in vivo. Compared to NONO WT cells, NONO R251K mutant-expressing CRC cells showed reduced proliferation, migration, and invasion, and PRMT1 knockdown or pharmacological inhibition abrogated the malignant phenotype associated with NONO asymmetric dimethylation in both KRAS WT and mutant CRC cells. Compared to adjacent normal tissue, PRMT1 was highly expressed in the CRC zone in clinical specimens, which was correlated with poor overall survival in patients with locally advanced CRC. These results demonstrate that PRMT1-mediated methylation of NONO at R251 promotes CRC growth and metastasis, and suggest that PRMT1 inhibition may be an effective therapeutic strategy for CRC treatment regardless of KRAS mutation status.


Assuntos
Neoplasias Colorretais/genética , Proteínas de Ligação a DNA/genética , Proteína-Arginina N-Metiltransferases/genética , Proteínas Proto-Oncogênicas p21(ras)/genética , Proteínas de Ligação a RNA/genética , Proteínas Repressoras/genética , Animais , Arginina , Carcinogênese/genética , Movimento Celular/genética , Proliferação de Células/genética , Neoplasias Colorretais/patologia , Regulação Neoplásica da Expressão Gênica , Xenoenxertos , Humanos , Metilação , Camundongos
14.
Nanoscale Res Lett ; 8(1): 328, 2013 Jul 18.
Artigo em Inglês | MEDLINE | ID: mdl-23866967

RESUMO

Ag and Cu nanocrystals (NCs) were assembled into ordered porous anodic alumina (OPAA) by a single-potential-step chronoamperometry technique. The composition, morphology, microstructure, and optical property were analyzed by X-ray diffraction, field-emission scanning electron microscopy, transmission electron microscopy, selected area electron diffraction, and optical absorption spectroscopy. The results indicate that metallic NCs/OPAA composite possesses a significant surface plasmon resonance absorption. For continuous electrodeposition, metallic nanowires are smooth and uniform with face-centered cubic (fcc) single-crystalline structure; however, for interval electrodeposition, the nanowires are bamboo-like or pearl-chain-like with fcc polycrystalline structure. The length of the nanoparticle nanowires or the single-crystalline nanowires can be controlled well by adjusting the experimental cycle times or the continuous depositing time. The transverse dipole resonance of metallic NCs enhances and displays a blue shift with increasing electrodeposition time or experimental cycle times, which is consistent with Zong's results but contradictory to Duan's results. The formation mechanisms of the nanoparticle nanowires and the single-crystalline nanowires were discussed in detail.

15.
Vet Microbiol ; 156(1-2): 200-4, 2012 Apr 23.
Artigo em Inglês | MEDLINE | ID: mdl-22051445

RESUMO

The amino acid sequence (TAVSPTTLR, 829-837aa) on the glycoprotein E2 of classical swine fever virus (CSFV) is a conserved and linear neutralizing epitope. In the present study, two peptides were constructed based the core sequence of this neutralizing epitope, the dendrimeric peptide (Th-B(4)) containing four copies of B cell epitope fused to one copy of promiscuous T helper (Th) cell epitope and the peptide Th-B containing a single copy of B cell epitope fused to one copy of Th cell epitope. The dendrimeric peptide Th-B(4) elicited high titers of neutralizing antibodies as detected in an indirect ELISA, blocking ELISA and neutralization test and induced a complete protection against CSFV C strain in rabbits. The Th-B elicited low titers of neutralizing antibodies and did not induce a protection in rabbits. These results suggest that the dendrimeric peptide Th-B(4) may be a promising marker vaccine candidate against CSFV and the multimerization is a requirement for development of a peptide vaccine.


Assuntos
Vírus da Febre Suína Clássica/imunologia , Peste Suína Clássica/prevenção & controle , Vacinas Virais/imunologia , Animais , Anticorpos Neutralizantes , Anticorpos Antivirais/imunologia , Peste Suína Clássica/imunologia , Ensaio de Imunoadsorção Enzimática , Epitopos de Linfócito B/química , Epitopos de Linfócito B/imunologia , Testes de Neutralização , Coelhos , Suínos , Vacinas de Subunidades Antigênicas/química , Vacinas de Subunidades Antigênicas/imunologia , Proteínas do Envelope Viral/química , Proteínas do Envelope Viral/imunologia , Vacinas Virais/química
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