Characterization of the DNA and structural proteins of entomopoxviruses from Melanoplus sanguinipes, Arphia conspirsa, and Phoetaliotes nebrascensis (Orthoptera)

1983 ◽  
Vol 42 (3) ◽  
pp. 327-333 ◽  
Author(s):  
W.H.R. Langridge ◽  
E. Oma ◽  
J.E. Henry
Author(s):  
Neha Periwal ◽  
Shravan B. Rathod ◽  
Ranjan Pal ◽  
Priya Sharma ◽  
Lata Nebhnani ◽  
...  

Pathogens ◽  
2021 ◽  
Vol 10 (6) ◽  
pp. 771
Author(s):  
Autumn T. LaPointe ◽  
Kevin J. Sokoloski

Alphaviruses are positive-sense RNA arboviruses that are capable of causing severe disease in otherwise healthy individuals. There are many aspects of viral infection that determine pathogenesis and major efforts regarding the identification and characterization of virulence determinants have largely focused on the roles of the nonstructural and structural proteins. Nonetheless, the viral RNAs of the alphaviruses themselves play important roles in regard to virulence and pathogenesis. In particular, many sequences and secondary structures within the viral RNAs play an important part in the development of disease and may be considered important determinants of virulence. In this review article, we summarize the known RNA-based virulence traits and host:RNA interactions that influence alphaviral pathogenesis for each of the viral RNA species produced during infection. Overall, the viral RNAs produced during infection are important contributors to alphaviral pathogenesis and more research is needed to fully understand how each RNA species impacts the host response to infection as well as the development of disease.


2017 ◽  
Vol 144 ◽  
pp. 18-23 ◽  
Author(s):  
Peng Lü ◽  
Yali Xing ◽  
Zhaoyang Hu ◽  
Yanhua Yang ◽  
Ye Pan ◽  
...  

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Agnieszka Biernatowska ◽  
Paulina Olszewska ◽  
Krzysztof Grzymajło ◽  
Dominik Drabik ◽  
Sebastian Kraszewski ◽  
...  

AbstractFlotillins are the major structural proteins in erythroid raft domains. We have shown previously that the dynamic nanoscale organization of raft domains in erythroid cells may depend on flotillin-MPP1 interactions. Here, by using molecular dynamic simulations and a surface plasmon resonance-based approach we determined that high-affinity complexes of MPP1 and flotillins are formed via a so far unidentified region within the D5 domain of MPP1. Significantly, this particular “flotillin binding motif” is of key physiological importance, as overexpression of peptides containing this motif inhibited endogenous MPP1-flotillin interaction in erythroid precursor cells, thereby causing lateral disorganization of raft domains. This was reflected by both reduction in the plasma membrane order and markedly decreased activation of signal transduction via the raft-dependent insulin receptor pathway. Our data highlight new molecular details concerning the mechanism whereby MPP1 functionally links flotillins to exert their physiological role in raft domain formation.


Author(s):  
Janneke J. M. Meulenberg ◽  
Annelien Petersen-den Besten ◽  
Eric P. de Kluyver ◽  
Rob J. M. Moormann ◽  
Wim M. M. Schaaper ◽  
...  

1996 ◽  
Vol 70 (1) ◽  
pp. 207-216 ◽  
Author(s):  
S Jameel ◽  
M Zafrullah ◽  
M H Ozdener ◽  
S K Panda

Parasitology ◽  
2012 ◽  
Vol 139 (9) ◽  
pp. 1178-1194 ◽  
Author(s):  
R. ALAN WILSON

SUMMARYSince 2004 there has been a remarkable increment in our knowledge of the proteins and glycans that reside at, or are released from the surfaces of schistosomes in the mammalian host. Initial characterization of the soluble proteome permits distinctions to be made between the parasite secretome and its necrotome. The principal proteins secreted by the cercaria to gain access to the skin have been described as well as those released by migrating schistosomula. An inventory of transporters, enzymes and structural proteins has been shown to reside the tegument surface, but also immunoglobulins, complement factors and host CD44. The secreted membranocalyx that overlies the plasma membrane may contain a small number of proteins, not simply acting as physical barrier, but its lipid composition remains elusive. Analysis of worm vomitus has provided insights into blood feeding, increasing the number of known lysosomal hydrolases, and identifying a series of carrier proteins potentially involved in uptake of lipids and inorganic ions by the gut epithelium. The egg secretions that aid escape from the tissues include a mixture of MEG-2 and MEG-3 family variant proteins. The utility of identified proteins for the development of new diagnostics, and their potential as vaccines candidates is evaluated.


1985 ◽  
Vol 3 ◽  
pp. 61
Author(s):  
Robert Rydbeck ◽  
Claes Örvell ◽  
Arthur Löve ◽  
Erling Norrby

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