Uriel Mauricio Valdez-Espinoza

Dr. Uriel Mauricio Valdez-Espinoza

orcid

Research Focus & Metrics

Academic Career Length

9Years (2018-Present)

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

Representative Publications

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3 July 2025 in Scientific Reports
Verified
Journal Article
Open access
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UVUriel Mauricio Valdez-Espinoza
Uriel Mauricio Valdez-Espinoza
LFLucas A. Fadda
Lucas A. Fadda
RMRoberta Marques
Roberta Marques
LOLuis Osorio-Olvera
Luis Osorio-Olvera
DJDaniel Jiménez-García
Daniel Jiménez-García
ALAndres Lira-Noriega
Andres Lira-Noriega
The reemergence of the New World screwworm (Cochliomyia hominivorax) poses a significant threat to animal and public health with minimal regulatory oversight. This study analyzes the potential distribution and reemergence of this pest, which is endemic to South America but was previously eradicated in North America. We first developed bioclimatic suitability models, and then incorporated these findings along with reemergence records and inspection point data to simulate possible dispersal routes into Mexico and the United States. Our results document the historical distribution of C. hominivorax across the Americas and recent reemergence events in Panama (2023) and Mexico (2024–2025). Findings indicate high invasion potential from Central America, with significant risk along Mexico’s Pacific and Atlantic coasts and the Yucatan Peninsula. In the United States, Texas and Florida face the highest risk. Regions with high livestock density in both countries demonstrate considerable climatic suitability for the pest. Our simulations identify Chiapas, Campeche, Tabasco, and Veracruz as critical northern dispersal points. The invadable areas contain substantial populations of domestic hosts, primarily cattle and horses. These findings will enable governmental authorities to develop comprehensive prevention and control strategies to address this emerging threat.

15 September 2022 in Ticks and Tick-borne Diseases
Verified
Journal Article
Closed access
Rodolfo Lagunes-QuintanillaRodolfo Lagunes-Quintanilla
Rodolfo Lagunes-Quintanilla
UVUriel Mauricio Valdez-Espinoza
Uriel Mauricio Valdez-Espinoza
RHRUBEN HERNANDEZ-ORTIZ
RUBEN HERNANDEZ-ORTIZ
ECEdgar Castro-Saines
Edgar Castro-Saines
OMOctavio Merino
Octavio Merino
NMNancy Mendoza-Martínez
Nancy Mendoza-Martínez

16 July 2025 in Medical and Veterinary Entomology
Verified
Journal Article
Closed access
UVUriel Mauricio Valdez-Espinoza
Uriel Mauricio Valdez-Espinoza
DSDiego SANTIAGO Santiago-Alarcon
Diego SANTIAGO Santiago-Alarcon
FVFabricio Villalobos
Fabricio Villalobos
RMRoberta Marques
Roberta Marques
Rodolfo Lagunes-QuintanillaRodolfo Lagunes-Quintanilla
Rodolfo Lagunes-Quintanilla
ALAndres Lira-Noriega
Andres Lira-Noriega

23 March 2018 in Veterinary Sciences
Verified
Journal Article
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DHDiego Josimar Hernández-Silva
Diego Josimar Hernández-Silva
UVUriel Mauricio Valdez-Espinoza
Uriel Mauricio Valdez-Espinoza
MMMiguel Angel Mercado-Uriostegui
Miguel Angel Mercado-Uriostegui
GAGabriela Aguilar-Tipacamú
Gabriela Aguilar-Tipacamú
JRJuan Alberto Ramos-Aragón
Juan Alberto Ramos-Aragón
Juan MosquedaJuan Mosqueda
Juan Mosqueda
Babesia bigemina is one of the most prevalent species causing bovine babesiosis around the world. Antigens involved in host cell invasion are vaccine targets for this disease but are largely unknown in this species. The invasion process of Babesia spp. into erythrocytes involves membrane proteins from the apical complex. A protein stored in the micronemes, called Micronemal Protein 1 (MIC-1), contains a sialic acid binding domain that participates in the invasion process of host cells and is a vaccine candidate in other apicomplexan parasites. It is not known if there is a homologous gene for mic-1 in B. bigemina. Therefore, the aim of this study was to characterize the mic-1 gene homologue in Babesia bigemina. A gene was found with a microneme adhesive repeat (MAR) domain in the predicted amino acid sequence. Transcription was determined by reverse transcription polymerase chain reaction (RT-PCR). Subsequently, antibodies against peptides containing conserved B-cell epitopes were used to confirm the expression of MIC-1 in intraerythrocytic merozoites. The presence of anti MIC-1 antibodies in cattle naturally infected with B. bigemina was determined and up to 97.4% of the cattle sera (113 out of 116) identified MIC-1 using enzyme-linked immunosorbent assay (ELISA) methods. Finally, antibodies against MIC-1 were able to block 70% merozoite invasion in-vitro.

18 May 2022 in Pathogens
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Journal Article
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MMMiguel Angel Mercado-Uriostegui
Miguel Angel Mercado-Uriostegui
Luis Castro-SánchezLuis Castro-Sánchez
Luis Castro-Sánchez
Gaber El-Saber BatihaGaber El-Saber Batiha
Gaber El-Saber Batiha
UVUriel Mauricio Valdez-Espinoza
Uriel Mauricio Valdez-Espinoza
AFAlfonso Falcón-Neri
Alfonso Falcón-Neri
Juan MosquedaJuan Mosqueda
Juan Mosqueda
In B. bigemina, the 45 kilodaltons glycoprotein (GP-45) is the most studied. GP-45 is exposed on the surface of the B. bigemina merozoite, it is believed to play a role in the invasion of erythrocytes, and it is characterized by a high genetic and antigenic polymorphism. The objective of this study was to determine if GP-45 contains conserved B-cell epitopes, and if they would induce neutralizing antibodies. The comparative analysis of nucleotide and amino acids sequences revealed a high percentage of similarity between field isolates. Antibodies against peptides containing conserved B-cell epitopes of GP-45 were generated. Antibodies present in the sera of mice immunized with GP-45 peptides specifically recognize B. bigemina by the IFAT. More than 95% of cattle naturally infected with B. bigemina contained antibodies against conserved GP-45 peptides tested by ELISA. Finally, sera from rabbits immunized with GP-45 peptides were evaluated in vitro neutralization tests and it was shown that they reduced the percentage of parasitemia compared to sera from rabbits immunized with adjuvant. GP-45 from geographically distant isolates of B. bigemina contains conserved B-cell epitopes that induce neutralizing antibodies suggesting that this gene and its product play a critical role in the survival of the parasite under field conditions.

22 March 2023 in Pathogens
Verified
Journal Article
Open access
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Juan MosquedaJuan Mosqueda
Juan Mosqueda
DHDiego Josimar Hernandez-Silva
Diego Josimar Hernandez-Silva
MUMassaro Ueti
Massaro Ueti
ACAdolfo Cruz-Reséndiz
Adolfo Cruz-Reséndiz
RMRicardo Marquez-Cervantez
Ricardo Marquez-Cervantez
Ikuo IgarashiIkuo Igarashi
Ikuo Igarashi
Bovine babesiosis is a tick-transmitted disease caused by intraerythrocytic protozoan parasites of the genus Babesia. Its main causative agents in the Americas are Babesia bigemina and Babesia bovis, while Babesia ovata affects cattle in Asia. All Babesia species secrete proteins stored in organelles of the apical complex, which are involved in all steps of the invasion process of vertebrate host cells. Unlike other apicomplexans, which have dense granules, babesia parasites instead have large, round intracellular organelles called spherical bodies. Evidence suggests that proteins from these organelles are released during the process of invading red blood cells, where spherical body proteins (SBPs) play an important role in cytoskeleton reorganization. In this study, we characterized the gene that encodes SBP4 in B. bigemina. This gene is transcribed and expressed in the erythrocytic stages of B. bigemina. The sbp4 gene consists of 834 nucleotides without introns that encode a protein of 277 amino acids. In silico analysis predicted a signal peptide that is cleaved at residue 20, producing a 28.88-kDa protein. The presence of a signal peptide and the absence of transmembrane domains suggest that this protein is secreted. Importantly, when cattle were immunized with recombinant B. bigemina SBP4, antibodies identified B. bigemina and B. ovata merozoites according to confocal microscopy observations and were able to neutralize parasite multiplication in vitro for both species. Four peptides with predicted B-cell epitopes were identified to be conserved in 17 different isolates from six countries. Compared with the pre-immunization sera, antibodies against these conserved peptides reduced parasite invasion in vitro by 57%, 44%, 42%, and 38% for peptides 1, 2, 3, and 4, respectively (p < 0.05). Moreover, sera from cattle infected with B. bigemina cattle contained antibodies that recognized the individual peptides. All these results support the concept of spb4 as a new gene in B. bigemina that should be considered a candidate for a vaccine to control bovine babesiosis.