scholarly journals A novel form of oxytocin in New World monkeys

2011 ◽  
Vol 7 (4) ◽  
pp. 584-587 ◽  
Author(s):  
Alex G. Lee ◽  
David R. Cool ◽  
William C. Grunwald ◽  
Donald E. Neal ◽  
Christine L. Buckmaster ◽  
...  

Oxytocin is widely believed to be present and structurally identical in all placental mammals. Here, we report that multiple species of New World monkeys possess a novel form of oxytocin, [P8] oxytocin. This mutation arises from a substitution of a leucine to a proline in amino acid position 8. Further analysis of this mutation in Saimiri sciureus (squirrel monkey) indicates that [P8] oxytocin is transcribed and translated properly. This mutation is specific to oxytocin, as the peptide sequence for arginine vasopressin, a structurally related nonapeptide, is unaltered. These findings dispel the notion that all placental mammals possess a ‘universal’ oxytocin sequence, and highlight the need for research on the functional significance of this novel nonapeptide in New World monkeys.

1969 ◽  
Vol 6 (6) ◽  
pp. 481-486 ◽  
Author(s):  
H. W. Moon ◽  
D. M. Barnes ◽  
J. M. Higbee

Infection with Actinobacillus equuli occurred in a squirrel monkey ( Saimiri sciureus) and a spider monkey ( Ateles paniscus). The disease in monkeys, characterized by widespread bacterial embolism and embolic suppurative nephritis, was similar to the disease caused by A. equuli in foals.


2005 ◽  
Vol 119 (4) ◽  
pp. 461-464 ◽  
Author(s):  
James R. Anderson ◽  
Hika Kuroshima ◽  
Yuko Hattori ◽  
Kazuo Fujita

PLoS ONE ◽  
2020 ◽  
Vol 15 (11) ◽  
pp. e0241487
Author(s):  
Délia Cristina Figueira Aguiar ◽  
Washington Luiz Assunção Pereira ◽  
Gyselly de Cássia Bastos de Matos ◽  
Klena Sarges Marruaz da Silva ◽  
Rosane do Socorro Pompeu de Loiola ◽  
...  

ABH antigens are histo-antigens, but were first described on the surface of human erythrocytes. They are found in those cells only in great apes and humans, while in more primitive animals they are found in tissues and body fluids. ABH antigens are mainly distributed in tissues that are in contact with the external environment and may serve as ligands for pathogens in tissues or block their connection. Description of the distribution of these molecules in non-human primate tissues is restricted to a few tissues and species. This paper describes the expression of human A, B and H type antigens in different organs from four species of New World Primates, obtained from the Centro Nacional de Primatas, as well as comparing that expression with what has been described for humans. In this study, although the tissue description of the antigens is similar to the genetic model for humans, some differences in expression between some organs from those species and those of humans were found. The differences occurred mainly in endodermal organs that have secretory functions and are probably under the control of the human-type FUT-2 enzyme. In the mesodermal-origin organs there was a reduction or absence of A and B antigen marking, particularly in the H precursor substance, indicating that those organs are under the control of the human-type FUT-1 enzyme. These findings have demonstrated that there is similar ABH antigen reactivity in tissue distribution between the species, although there are some species-specific cases.


2002 ◽  
Vol 76 (10) ◽  
pp. 5140-5146 ◽  
Author(s):  
Christina F. Spiropoulou ◽  
Stefan Kunz ◽  
Pierre E. Rollin ◽  
Kevin P. Campbell ◽  
Michael B. A. Oldstone

ABSTRACT α-Dystroglycan (α-DG) has been identified as a major receptor for lymphocytic choriomeningitis virus (LCMV) and Lassa virus, two Old World arenaviruses. The situation with New World arenaviruses is less clear: previous studies demonstrated that Oliveros virus also exhibited high-affinity binding to α-DG but that Guanarito virus did not. To extend these initial studies, several additional Old and New World arenaviruses were screened for entry into mouse embryonic stem cells possessing or lacking α-DG. In addition, representative viruses were further analyzed for direct binding to α-DG by means of a virus overlay protein blot assay technique. These studies indicate that Old World arenaviruses use α-DG as a major receptor, whereas, of the New World arenaviruses, only clade C viruses (i.e., Oliveros and Latino viruses) use α-DG as a major receptor. New World clade A and B arenaviruses, which include the highly pathogenic Machupo, Guanarito, Junin, and Sabia viruses, appear to use a different receptor or coreceptor for binding. Previous studies with LCMV have suggested the need for a small aliphatic amino acid at LCMV GP1 glycoprotein amino acid position 260 to allow high-affinity binding to α-DG. As reported herein, this requirement appears to be broadly applicable to the arenaviruses as determined by more extensive analysis of α-DG receptor usage and GP1 sequences of Old and New World arenaviruses. In addition, GP1 amino acid position 259 also appears to be important, since all arenaviruses showing high-affinity α-DG binding possess a bulky aromatic amino acid (tyrosine or phenylalanine) at this position.


2018 ◽  
Vol 92 (18) ◽  
Author(s):  
Samantha James ◽  
Damien Donato ◽  
Jean-François Pouliquen ◽  
Manuel Ruiz-García ◽  
Anne Lavergne ◽  
...  

ABSTRACTOver the past few decades, a large number of studies have identified herpesvirus sequences from many mammalian species around the world. Among the different nonhuman primate species tested so far for cytomegaloviruses (CMVs), only a few were from the New World. Seeking to identify CMV homologues in New World monkeys (NWMs), we carried out molecular screening of 244 blood DNA samples from 20 NWM species from Central and South America. Our aim was to reach a better understanding of their evolutionary processes within the Platyrrhini parvorder. Using PCR amplification with degenerate consensus primers targeting highly conserved amino acid motifs encoded by the herpesvirus DNA polymerase gene, we characterized novel viral sequences from 12 species belonging to seven genera representative of the three NWM families. BLAST searches, pairwise nucleotide and amino acid sequence comparisons, and phylogenetic analyses confirmed that they all belonged to theCytomegalovirusgenus. Previously determined host taxa allowed us to demonstrate a good correlation between the distinct monophyletic clades of viruses and those of the infected primates at the genus level. In addition, the evolutionary branching points that separate NWM CMVs were congruent with the divergence dates of their hosts at the genus level. These results significantly expand our knowledge of the host range of this viral genus and strongly support the occurrence of cospeciation between these viruses and their hosts. In this respect, we propose that NWM CMV DNA polymerase gene sequences may serve as reliable molecular markers with which to infer Platyrrhini phylogenetics.IMPORTANCEInvestigating evolutionary processes between viruses and nonhuman primates has led to the discovery of a large number of herpesviruses. No study published so far on primate cytomegaloviruses has extensively studied New World monkeys (NWMs) at the subspecies, species, genus, and family levels. The present study sought to identify cytomegalovirus homologues in NWMs and to decipher their evolutionary relationships. This led us to characterize novel viruses from 12 of the 20 primate species tested, which are representative of the three NWM families. The identification of distinct viruses in these primates not only significantly expands our knowledge of the host range of this viral genus but also sheds light on its evolutionary history. Phylogenetic analyses and molecular dating of the sequences obtained support a virus-host coevolution.


PLoS ONE ◽  
2021 ◽  
Vol 16 (10) ◽  
pp. e0259504
Author(s):  
Délia Cristina Figueira Aguiar ◽  
Washington Luiz Assunção Pereira ◽  
Gyselly de Cássia Bastos de Matos ◽  
Klena Sarges Marruaz da Silva ◽  
Rosane do Socorro Pompeu de Loiola ◽  
...  

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