Alexis Musacchio

Centro de Ingeniería Genética y Biotecnología

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Nelson Acosta‐Rivero

Centro de Ingeniería Genética y Biotecnología

Viviana Falcón

Centro de Ingeniería Genética y Biotecnología

Yasser Perera

Centro de Ingeniería Genética y Biotecnología

Ivis Guerra

Centro de Ingeniería Genética y Biotecnología

Amilcar Pérez-Riverol

University of Giessen

Gerardo Guillén

Centro de Ingeniería Genética y Biotecnología

Mário Sérgio Palma

Universidade Estadual Paulista (Unesp)

Yadira Lobaina

Centro de Ingeniería Genética y Biotecnología

Santiago Dueñas‐Carrera

Centro de Ingeniería Genética y Biotecnología

Glay Chinea

Centro de Ingeniería Genética y Biotecnología

Cooperative Institutions

Centro de Ingeniería Genética y Biotecnología

268

National Center for Genetic Engineering and Biotechnology

University of Havana

ORCID

Cuban Neuroscience Center

Center of Molecular Immunology (Cuba)

Finlay Institute

National University of Quilmes

Centre National de la Recherche Scientifique

Universidad Nacional Autónoma de México

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Hepatitis C virus: new lights on the horizon

Biotecnología aplicada (2004)

Santiago Dueñas Carrera Alexis Musacchio

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Diversity of peptidic and proteinaceous toxins from social Hymenoptera venoms

Toxicon (2018)

José Roberto Aparecido dos Santos‐Pinto Amilcar Pérez-Riverol Alexis Musacchio Mário Sérgio Palma

Fire ant

Biopesticide

10.1016/j.toxicon.2018.04.029

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Citations (68)

Redesignation of a Purported P1.15 Subtype-Specific Meningococcal Monoclonal Antibody as a P1.19-Specific Reagent

Clinical and Diagnostic Laboratory Immunology (1999)

Elisabeth Wedege Dominique A. Caugant Alexis Musacchio Nancy B. Saunders Wendell D. Zollinger

ABSTRACT Two reference monoclonal antibodies against the meningococcal P1.15 subtype PorA, MN3C5C and 2-1-P1.15, showed only partial concordant recognition of meningococcal isolates. Cyanogen bromide cleavage of P1.19,15 PorA, peptide mapping, and sequencing of porA regions demonstrated that 2-1-P1.15 was specific for subtype P1.19, and henceforth it is to be redesignated as 2-1-P1.19.

Cyanogen bromide

Cleavage (geology)

10.1128/cdli.6.4.639-642.1999

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Citations (6)

Obtención y caracterización bioquímica e inmunológica de la proteína recombinante Opc de Neisseria meningitidis. Demostración de su capacidad como proteína portadora para inmunización con ADN

Biotecnología aplicada (2003)

Alexis Musacchio Tania Carmenate Circe Mesa Daniela Quintana Segundo González

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A recombinant SARS-CoV-2 receptor-binding domain expressed in an engineered fungal strain of Thermothelomyces heterothallica induces a functional immune response in mice

Vaccine (2022)

Laura Lazo Mónica Béquet‐Romero Gilda Lemos Alexis Musacchio Ania Cabrales

Strain (injury)

10.1016/j.vaccine.2022.01.007

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Citations (14)

Fructan Biosynthesis in Bacteria

Caister Academic Press eBooks (2019)

Lázaro Hernández Yamira Quintero Alexis Musacchio

Fructan

10.21775/9781912530267.06

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Citations (2)

Recombinant in vitro assembled hepatitis C virus core particles induce strong specific immunity enhanced by formulation with an oil-based adjuvant

Biological Research (2009)

Nelson Acosta‐Rivero Joanna Poutou Liz Alvarez‐Lajonchere Ivis Guerra Yaraima Aguilera

In the present work, immunogenicity of recombinant in vitro assembled hepatitis C virus core particles, HCcAg.120-VLPs,either alone or in combination with different adjuvants was evaluated in BALB/c mice.HCcAg.120-VLPsinduced high titers of anti-HCcAg.120antibodies and virus-specific cellular immune responses.Particularly, HCcAg.120-VLPsinduced specific delayed type hypersensitivity, and generated a predominant T helper 1 cytokine profile in immunized mice.In addition, HCcAg.120-VLPsprime splenocytes proliferate in vitro against different HCcAg.120-specificpeptides, depending on either the immunization route or the adjuvant used.Remarkably, immunization with HCcAg.120-VLPs/MontanideISA888 formulation resulted in a significant control of vaccinia virus titer in mice after challenge with a recombinant vaccinia virus expressing HCV core protein, vvCore.Animals immunized with this formulation had a marked increase in the number of IFN-γ producing spleen cells, after stimulation with P815 cells infected with vvCore.These results suggest the use of recombinant HCV core particles as components of therapeutic or preventive vaccine candidates against HCV.

10.4067/s0716-97602009000100005

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Citations (17)

Ratio of HCV structural antigens in protein‐based vaccine formulations is critical for functional immune response induction

Biotechnology and Applied Biochemistry (2010)

Gillian Martínez‐Donato Alexis Musacchio Liz Alvarez‐Lajonchere Nelson Acosta‐Rivero Yalena Amador

HCV (hepatitis C virus) infection is among the leading causes of chronic liver disease, but currently there is no vaccine available. Data have accumulated about the importance of targeting different HCV antigens in vaccine candidate preparations. Here, a surface response study to select the optimal ratio of recombinant HCV structural antigens in a vaccine preparation, capable of generating in vivo functional cellular immune response in mice, was performed. The immunogenicity of the selected HCV structural protein mixture (Co–E1–E2) in mice and African green monkeys, after five doses of immunization, was also demonstrated. Specific T‐cell proliferative response against HCV structural antigens was induced in vaccinated mice. Moreover, on challenge with recombinant HCV VV (vaccinia virus), all mice controlled the viraemia and 80% were protected. On the other hand, monkeys immunized with Co–E1–E2 developed antibodies, specifically directed to region 412–438 of E2 protein, that include an epitope implicated in HCV neutralization, in addition to a specific proliferative response against HCV Core and E2 proteins. These results indicated that the optimal amount and ratio of HCV recombinant proteins should be taken into account to elicit a successful immune response against HCV and therefore have important implications for vaccine design.

10.1042/ba20090216

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Citations (8)

Increased antiviral activity of microscale‐purified _HuIFN_α8 (human interferon α8) over _HuIFN_α2b in Hep‐2 cells challenged with Mengo virus

Biotechnology and Applied Biochemistry (2007)

Julio César Sánchez García Alejandro Miranda Ariza Alexis Musacchio Luis Javier González Vladimir Besada Perez

Human proteins are not routinely expressed at high levels in Escherichia coli for, among other reasons, different codon usage. Several purification procedures have been applied to recover recombinant proteins for further biological characterization. However, the vast majority involve costly chromatography procedures. In the present study, both (Hu)IFN(alpha 2b) (human interferon alpha 2b) and (Hu)IFN(alpha 8) were expressed efficiently in E. coli BL21-codonplus-RIL. Subsequently, both recombinant proteins were purified to homogeneity by passive elution from reverse-stained SDS/PAGE gels, a cost-effective purification procedure. After purification, both recovered proteins were biologically active. The (Hu)IFN(alpha 8) subtype induced 1.46-fold more antiviral activity than (Hu)IFN(alpha 2b) using Hep-2 human laryngeal carcinoma cell challenged with Mengo virus.

Interferon alfa

10.1042/ba20060211

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Citations (4)

Characterisation of thelpdAgene fromNeisseria meningitidisby polymerase chain reaction, restriction fragment length polymorphism and sequencing

FEMS Microbiology Letters (1999)

P64k protein from Neisseria meningitidis is well recognised in sera from individuals convalescent from meningococcal disease or vaccinated with the Cuban antimeningococcal vaccine VA-MENGOC-BC®. The presence of the protein in more than 80 meningococcal strains has also been verified. It is immunogenic in animal models and the antibodies elicited show bactericidal activity against meningococci. To further investigate at the molecular level whether lpdA, the gene coding for P64k protein, is conserved among different N. meningitidis strains, a total of 20 strains isolated from different geographic areas were differentiated on the basis of restriction fragment length polymorphism (RFLP) patterns after polymerase chain reaction (PCR) amplification of the lpdA gene and restriction endonuclease digestion with HpaII. Although a total of five different PCR-RFLP patterns were present, nucleotide sequence determination showed that identity levels were as high as 93–99% among the N. meningitidis strains analysed.

Neisseria

Restriction fragment

10.1111/j.1574-6968.1999.tb13568.x

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Citations (11)