Marco V. José

Prof. Marco V. José

orcid

Research Focus & Metrics

Academic Career Length

27Years (2000-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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20 September 2017 in Frontiers in Genetics
Verified
Journal Article
Open access
SFSávio Farias
Sávio Farias
AJAriosvaldo P. dos Santos Junior
Ariosvaldo P. dos Santos Junior
TGThais Gaudencio
Thais Gaudencio
MJMarco V. José
Marco V. José
RNA-dependent RNA polymerases (RdRp) are very ancient enzymes and are essential for all viruses with RNA genomes. We reconstruct the origin and evolution of this polymerase since the initial stages of the origin of life. The origin of the RdRp was traced back from tRNA ancestors. At the origin of the RdRp the most ancient part of the protein is the cofactor binding site that had the capacity of binding to simple molecules as magnesium, calcium and ribonucleotides. Our results suggest that RdRp originated from junctions of proto-tRNAs that worked as the first genes at the emergence of the primitive translation system, where the RNA was the informational molecule. The initial domain, worked as a building block for the emergence of the fingers and thumb domains. From the ancestral RdRp, we could establish the evolutionary stages of viral evolution from a rooted ancestor to modern viruses. It was observed that the selective pressure under the RdRp was the organization and functioning of the genome, where RNA double stranded and RNA single stranded virus formed a separate group. We propose an evolutionary route to the polymerases and the results suggest an ancient scenario for the origin of RNA viruses.

1 January 2014 in FEBS Open Bio
Verified
Journal Article
Open access
SFSávio Farias
Sávio Farias
TGThais Gaudencio
Thais Gaudencio
MJMarco V. José
Marco V. José
We tested the hypothesis of Tamura (2011) [3] that molecules of tRNA gave origin to ribosomes, particularly to the Peptidyl Transferase Center (PTC) of the 23S ribosomal RNA. We reconstructed the ancestral sequences from all types of tRNA and compared them in their sequences with the current PTC of 23S ribosomal RNA from different organisms. We built an ancestral sequence of proto‐tRNAs that showed a remarkable overall identity of 50.53% with the catalytic site of PTC. We conclude that the Peptidyl Transferase Center was indeed originated by the fusion of ancestral sequences of proto‐tRNA.

23 March 2016 in Life
Verified
Journal Article
Open access
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SFSávio Farias
Sávio Farias
TGThais Gaudencio
Thais Gaudencio
MJMarco V. José
Marco V. José
Herein we present the tRNA core hypothesis, which emphasizes the central role of tRNAs molecules in the origin and evolution of fundamental biological processes. tRNAs gave origin to the first genes (mRNA) and the peptidyl transferase center (rRNA), proto-tRNAs were at the core of a proto-translation system, and the anticodon and operational codes then arose in tRNAs molecules. Metabolic pathways emerged from evolutionary pressures of the decoding systems. The transitions from the RNA world to the ribonucleoprotein world to modern biological systems were driven by three kinds of tRNAs transitions, to wit, tRNAs leading to both mRNA and rRNA.

24 February 2021 in Frontiers in Immunology
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Journal Article
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EREdgar Ramos-Martínez
Edgar Ramos-Martínez
LHLeticia Hernández-González
Leticia Hernández-González
IRIván Ramos-Martínez
Iván Ramos-Martínez
Laura Pérez-Campos MayoralLaura Pérez-Campos Mayoral
Laura Pérez-Campos Mayoral
GLGeorgina I. López-Cortés
Georgina I. López-Cortés
MJMarco V. José
Marco V. José
Extracellular DNA traps (ETs) are evolutionarily conserved antimicrobial mechanisms present in protozoa, plants, and animals. In this review, we compare their similarities in species of different taxa, and put forward the hypothesis that ETs have multiple origins. Our results are consistent with a process of evolutionary convergence in multicellular organisms through the application of a congruency test. Furthermore, we discuss why multicellularity is related to the presence of a mechanism initiating the formation of ETs.

28 May 2022 in Vaccines
Verified
Journal Article
Open access
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GLGeorgina I. López-Cortés
Georgina I. López-Cortés
Miryam Palacios-PérezMiryam Palacios-Pérez
Miryam Palacios-Pérez
HVHannya F. Veledíaz
Hannya F. Veledíaz
MHMargarita Hernández-Aguilar
Margarita Hernández-Aguilar
GLGerardo R. López-Hernández
Gerardo R. López-Hernández
MJMarco V. José
Marco V. José
The global scale of the COVID-19 pandemic has demonstrated the evolution of SARS-CoV-2 and the clues of adaptation. After two years and two months since the declaration of the pandemic, several variants have emerged and become fixed in the human population thanks to extrinsic selective pressures but also to the inherent mutational capacity of the virus. Here, we applied a neutral substitution evolution test to the spike (S) protein of Omicron’s protein and compared it to the others’ variant of concern (VOC) neutral evolution. We carried out comparisons among the interactions between the S proteins from the VOCs (Alpha, Beta, Gamma, Delta and Omicron) and the receptor ACE2. The shared amino acids among all the ACE2 binding S proteins remain constant, indicating that these amino acids are essential for the accurate binding to the receptor. The complexes of the RBD for every variant with the receptor were used to identify the amino acids involved in the protein—protein interaction (PPI). The RBD of Omicron establishes 82 contacts, compared to the 74 of the Wuhan original viral protein. Hence, the mean number of contacts per residue is higher, making the contact thermodynamically more stable. The RBDs of the VOCs are similar in sequence and structure; however, Omicron’s RBD presents the largest deviation from the structure by 1.11 Å RMSD, caused by a set of mutations near the glycosylation N343. The chemical properties and structure near the glycosylation N343 of the Omicron S protein are different from the original protein, which provoke reduced recognition by the neutralizing antibodies. Our results hint that selective pressures are induced by mass vaccination throughout the world and by the persistence of recurrent infections in immunosuppressed individuals, who did not eliminate the infection and ended up facilitating the selection of viruses whose characteristics are different from the previous VOCs, less pathogenic but with higher transmissibility.

1 March 2017 in Royal Society Open Science
Verified
Journal Article
Open access
MJMarco V. José
Marco V. José
GZGabriel Zamudio
Gabriel Zamudio
EMEberto R. Morgado
Eberto R. Morgado
The Rodin–Ohno (RO) and the Delarue models divide the table of the genetic code into two classes of aminoacyl-tRNA synthetases (aaRSs I and II) with recognition from the minor or major groove sides of the tRNA acceptor stem, respectively. These models are asymmetric but they are biologically meaningful. On the other hand, the standard genetic code (SGC) can be derived from the primeval RNY code (R stands for purines, Y for pyrimidines and N any of them). In this work, the RO-model is derived by means of group actions, namely, symmetries represented by automorphisms, assuming that the SGC originated from a primeval RNY code. It turns out that the RO-model is symmetric in a six-dimensional (6D) hypercube. Conversely, using the same automorphisms, we show that the RO-model can lead to the SGC. In addition, the asymmetric Delarue model becomes symmetric by means of quotient group operations. We formulate isometric functions that convert the class aaRS I into the class aaRS II and vice versa. We show that the four polar requirement categories display a symmetrical arrangement in our 6D hypercube. Altogether these results cannot be attained, neither in two nor in three dimensions. We discuss the present unified 6D algebraic model, which is compatible with both the SGC (based upon the primeval RNY code) and the RO-model.