Identification and characterization of a novel specific secreted protein family for selected members of the subfamily Ostertagiinae (Nematoda)

Parasitology ◽  
2007 ◽  
Vol 135 (1) ◽  
pp. 63-70 ◽  
Author(s):  
H. SAVERWYNS ◽  
A. VISSER ◽  
A. J. NISBET ◽  
I. PEELAERS ◽  
K. GEVAERT ◽  
...  
Keyword(s):  
Developmental Stages ◽  
Cell Damage ◽  
Inflammatory Cells ◽  
Glycosylation Site ◽  
Protein Family ◽  
Protein Motif ◽  
Western Blots ◽  
Teladorsagia Circumcincta ◽  
Identification And Characterization

SUMMARYIt has been shown that the bovine abomasal parasite, Ostertagia ostertagi, drastically modulates its microenvironment, causing epithelial cell damage, accumulation of inflammatory cells and pH changes in the stomach. The mechanisms used by the parasite to change the abomasal environment are largely unknown, but an important role has been attributed to excretory-secretory (ES) products from the parasite. In this study we have identified proteins representing a novel ES protein family, characterized by the SCP/Tpx-1/Ag5/PR-1/Sc7 protein motif. These proteins were named Oo-AL1 and Oo-AL2 (O. ostertagi ASP-like protein). Both proteins contain a signal peptide and 1 predicted N-glycosylation site. The transcript for Oo-AL1 was present from the L4 stage onwards in both male and female adult worms, whereas the Oo-AL2 transcript was hardly detectable. Western blots of somatic extracts and ES products from different developmental stages of O. ostertagi, probed with anti-Oo-AL1 antibodies, revealed Oo-AL proteins in the ES products of adult worms. An analysis of the nematode genome and EST databases indicated that these novel ES proteins are unique to O. ostertagi and its relative, Teladorsagia circumcincta, suggesting a key function in these abomasal parasites.

scholarly journals Identification and Characterization of Four Autophagy-Related Genes That Are Expressed in Response to Hypoxia in the Brain of the Oriental River Prawn (Macrobrachium nipponense)

2019 ◽  
Vol 20 (8) ◽  
pp. 1856 ◽  
Author(s):  
Shengming Sun ◽  
Ying Wu ◽  
Hongtuo Fu ◽  
Xianping Ge ◽  
Hongzheng You ◽  
...  
Keyword(s):  
Developmental Stages ◽  
Open Reading Frames ◽  
Dependent Manner ◽  
Macrobrachium Nipponense ◽  
Oriental River Prawn ◽  
Adverse Environmental Conditions ◽  
The Brain ◽  
Identification And Characterization

Autophagy is a cytoprotective mechanism triggered in response to adverse environmental conditions. Herein, we investigated the autophagy process in the oriental river prawn (Macrobrachium nipponense) following hypoxia. Full-length cDNAs encoding autophagy-related genes (ATGs) ATG3, ATG4B, ATG5, and ATG9A were cloned, and transcription following hypoxia was explored in different tissues and developmental stages. The ATG3, ATG4B, ATG5, and ATG9A cDNAs include open reading frames encoding proteins of 319, 264, 268, and 828 amino acids, respectively. The four M. nipponense proteins clustered separately from vertebrate homologs in phylogenetic analysis. All four mRNAs were expressed in various tissues, with highest levels in brain and hepatopancreas. Hypoxia up-regulated all four mRNAs in a time-dependent manner. Thus, these genes may contribute to autophagy-based responses against hypoxia in M. nipponense. Biochemical analysis revealed that hypoxia stimulated anaerobic metabolism in the brain tissue. Furthermore, in situ hybridization experiments revealed that ATG4B was mainly expressed in the secretory and astrocyte cells of the brain. Silencing of ATG4B down-regulated ATG8 and decreased cell viability in juvenile prawn brains following hypoxia. Thus, autophagy is an adaptive response protecting against hypoxia in M. nipponense and possibly other crustaceans. Recombinant MnATG4B could interact with recombinant MnATG8, but the GST protein could not bind to MnATG8. These findings provide us with a better understanding of the fundamental mechanisms of autophagy in prawns.

Identification and characterization of rDJL, a novel member of the DnaJ protein family, in rat testis

FEBS Letters ◽  
2005 ◽  
Vol 579 (25) ◽  
pp. 5734-5740 ◽  
Author(s):  
Chunbo Yang ◽  
Shiying Miao ◽  
Shudong Zong ◽  
Samuel S. Koide ◽  
Linfang Wang
Keyword(s):  
Protein Family ◽  
Rat Testis ◽  
Dnaj Protein ◽  
Identification And Characterization

scholarly journals Differential Subcellular Localization of Members of the Toxoplasma gondii Small Heat Shock Protein Family

2005 ◽  
Vol 4 (12) ◽  
pp. 1990-1997 ◽  
Author(s):  
N. de Miguel ◽  
P. C. Echeverria ◽  
S. O. Angel
Keyword(s):  
Heat Shock ◽  
Toxoplasma Gondii ◽  
Heat Shock Protein ◽  
Subcellular Localization ◽  
Small Heat Shock Protein ◽  
Terminal Segment ◽  
Protein Family ◽  
Link Type ◽  
Identification And Characterization

ABSTRACT The results of this study describe the identification and characterization of the Toxoplasma gondii α-crystallin/small heat shock protein (sHsp) family. By database (www.toxodb.org ) search, five parasite sHsps (Hsp20, Hsp21, Hsp28, Hsp29, and the previously characterized Hsp30/Bag1) were identified. As expected, they share the homologous α-crystallin domain, which is the key characteristic of sHsps. However, the N-terminal segment of each protein contains unique characteristics in size and sequence. Most T. gondii sHsps are constitutively expressed in tachyzoites and fully differentiated bradyzoites, with the exception of Hsp30/Bag1. Interestingly, by subcellular localization we observed that T. gondii sHsps are located in different compartments. Hsp20 is located at the apical end of the cell, Hsp28 is located inside the mitochondrion, Hsp29 showed a membrane-associated labeling, and Hsp21 appeared throughout the cytosol of the parasites. These particular differences in the immunostaining patterns suggest that their targets and functions might be different.

scholarly journals Identification and characterization of the 2D6 and Mr 23000 antigens on the plasma membrane of rat spermatozoa

1987 ◽  
Vol 241 (2) ◽  
pp. 353-360 ◽  
Author(s):  
R Jones ◽  
C R Brown
Keyword(s):  
Plasma Membrane ◽  
Antigenic Determinant ◽  
Egg Recognition ◽  
Western Blots ◽  
One Dimensional ◽  
Antigen Present ◽  
Membrane Bound ◽  
Species Specific ◽  
Identification And Characterization

Previous investigations [Jones, Brown, von Glos & Gaunt (1985) Exp. Cell Res. 156, 31-44] have demonstrated the appearance of a new antigenic determinant (recognized by monoclonal antibody 2D6) on the plasma membrane of rat spermatozoa during post-testicular maturation in the epididymis. Identification of the 2D6 antigen on Western blots from one-dimensional SDS/polyacrylamide gels revealed that it co-migrated with a membrane protein (designated Mr 23,000 antigen) present on testicular and immature germ cells, suggesting that one antigen might be a modified version of the other. In the present work, however, we demonstrate that, although they have similar Mr and are present in soluble and membrane-bound forms, the 2D6 and Mr 23,000 antigens are biochemically and immunologically distinct molecules. The properties of the antigens are described and compared. The Mr 23,000 antigen is present on both testicular and cauda epididymidal spermatozoa, has a pI of 6.1, contains no detectable carbohydrate, is not tissue-specific and is degraded by V8 protease. By contrast, the 2D6 antigen is glycosylated, has a broad pI from 4.5 to 6.1, is tissue- and species-specific and is resistant to digestion with V8 protease. Its role in sperm-egg recognition is discussed.

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