Comparative study of the physicochemical properties of the species-specific proteins of cotton plants of the speciesGossypium hirsutum andG. barbadense

1995 ◽  
Vol 31 (6) ◽  
pp. 734-739
Author(s):  
A. M. �rmatov ◽  
D. A. Khashimov ◽  
P. Kh. Yuldshev
2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Arangasamy Yazhini ◽  
Narayanaswamy Srinivasan ◽  
Sankaran Sandhya

AbstractAfrotheria is a clade of African-origin species with striking dissimilarities in appearance and habitat. In this study, we compared whole proteome sequences of six Afrotherian species to obtain a broad viewpoint of their underlying molecular make-up, to recognize potentially unique proteomic signatures. We find that 62% of the proteomes studied here, predominantly involved in metabolism, are orthologous, while the number of homologous proteins between individual species is as high as 99.5%. Further, we find that among Afrotheria, L. africana has several orphan proteins with 112 proteins showing < 30% sequence identity with their homologues. Rigorous sequence searches and complementary approaches were employed to annotate 156 uncharacterized protein sequences and 28 species-specific proteins. For 122 proteins we predicted potential functional roles, 43 of which we associated with protein- and nucleic-acid binding roles. Further, we analysed domain content and variations in their combinations within Afrotheria and identified 141 unique functional domain architectures, highlighting proteins with potential for specialized functions. Finally, we discuss the potential relevance of highly represented protein families such as MAGE-B2, olfactory receptor and ribosomal proteins in L. africana and E. edwardii, respectively. Taken together, our study reports the first comparative study of the Afrotherian proteomes and highlights salient molecular features.


Molecules ◽  
2021 ◽  
Vol 26 (6) ◽  
pp. 1577
Author(s):  
Klaudia Kotecka-Majchrzak ◽  
Natalia Kasałka-Czarna ◽  
Agata Sumara ◽  
Emilia Fornal ◽  
Magdalena Montowska

Consumer demand for both plant products and meat products enriched with plant raw materials is constantly increasing. Therefore, new versatile and reliable methods are needed to find and combat fraudulent practices in processed foods. The objective of this study was to identify oilseed species-specific peptide markers and meat-specific markers that were resistant to processing, for multispecies authentication of different meat and vegan food products using the proteomic LC-MS/MS method. To assess the limit of detection (LOD) for hemp proteins, cooked meatballs consisting of three meat species and hemp cake at a final concentration of up to 7.4% were examined. Hemp addition at a low concentration of below 1% was detected. The LOD for edestin subunits and albumin was 0.9% (w/w), whereas for 7S vicilin-like protein it was 4.2% (w/w). Specific heat-stable peptides unique to hemp seeds, flaxseed, nigella, pumpkin, sesame, and sunflower seeds, as well as guinea fowl, rabbit, pork, and chicken meat, were detected in different meat and vegan foods. Most of the oilseed-specific peptides were identified as processing-resistant markers belonging to 11S globulin subunits, namely conlinin, edestin, helianthinin, pumpkin vicilin-like or late embryogenesis proteins, and sesame legumin-like as well as 2S albumins and oleosin isoforms or selected enzymic proteins.


Parasitology ◽  
2017 ◽  
Vol 144 (7) ◽  
pp. 851-868 ◽  
Author(s):  
LUÍS F. P. GONDIM ◽  
JOSÉ R. MINEO ◽  
GEREON SCHARES

SUMMARYToxoplasma gondii, Neosporaspp.,Sarcocystisspp.,Hammondiaspp. andBesnoitia besnoitiare genetically related cyst-forming coccidia. Serology is frequently used for the identification ofT. gondii, Neosporaspp. andB. besnoiti-exposed individuals. Serologic cross-reactions occur in different tests among animals infected withT. gondiiandH. hammondi,as well as among animals infected byT. gondiiandN. caninum. Infections caused byN. caninumandN. hughesiare almost indistinguishable by serology.Neospora caninum, B. besnoitiandSarcocystisspp. infections in cattle show some degree of serologic cross-reactivity. Antibody cross-reactivity betweenNeosporaspp. andH. heydorni-infected animals is suspected, but not proven to occur. We review serologic cross-reactivity among animals and/or humans infected withT. gondii, Neosporaspp.,Sarcocystisspp.,Hammondiaspp. andB. besnoiti. Emphasis is laid upon antigens and serological methods forN. caninumdiagnosis which were tested for cross-reactivity with related protozoa. Species-specific antigens, as well as stage-specific proteins have been identified in some of these parasites and have promising use for diagnosis and epidemiological surveys.


2012 ◽  
Vol 447 (1) ◽  
pp. 203-206 ◽  
Author(s):  
I. S. Ryzhkina ◽  
Yu. V. Kiseleva ◽  
L. I. Murtazina ◽  
O. A. Mishina ◽  
E. D. Sherman ◽  
...  

2021 ◽  
Author(s):  
Michael J Sheedlo ◽  
Clarissa L Durie ◽  
Jeong Min Chung ◽  
Louise Chang ◽  
Michele Swanson ◽  
...  

Legionella pneumophila is an opportunistic pathogen that causes the potentially fatal pneumonia known as Legionnaires’ Disease. The pathology associated with infection depends on bacterial delivery of effector proteins into the host via the membrane spanning Dot/Icm type IV secretion system (T4SS). We have determined sub-3.0 Å resolution maps of the Dot/Icm T4SS core complex by single particle cryo-EM. The high-resolution structural analysis has allowed us to identify proteins encoded outside the Dot/Icm genetic locus that contribute to the core T4SS structure. We can also now define two distinct areas of symmetry mismatch, one that connects the C18 periplasmic ring (PR) and the C13 outer membrane cap (OMC) and one that connects the C13 OMC with a 16-fold symmetric dome. Unexpectedly the connection between the PR and OMC is DotH, with five copies sandwiched between the OMC and PR to accommodate the symmetry mismatch. Finally, we observe multiple conformations in the reconstructions that indicate flexibility within the structure. We hypothesize this conformational flexibility is likely to facilitate the Dot/Icm T4SS’s ability to translocate a remarkably large set of ~300 putative substrates across the inner and outer membranes of the bacterial cell.


2020 ◽  
Vol 6 (2) ◽  
pp. 59-61
Author(s):  
Orole Regina Temitope ◽  
◽  
Orole Olukayode Olugbenga ◽  
Aisoni Japhet Erasmus ◽  
Isyaku Jamilu ◽  
...  

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