Only the First Steps of the Parallel Evolution Have Been Taken Thus Far

2012 ◽  
pp. 1-9 ◽  
Author(s):  
James Reinders
Keyword(s):  
Parallel Evolution

scholarly journals A Model-Based Approach for Adaptable Middleware Evolution in WSN Platforms

2021 ◽  
Vol 10 (1) ◽  
pp. 20
Author(s):  
Walter Tiberti ◽  
Dajana Cassioli ◽  
Antinisca Di Marco ◽  
Luigi Pomante ◽  
Marco Santic
Keyword(s):  
Wireless Sensor Networks ◽  
Sensor Networks ◽  
Embedded System ◽  
Operating Systems ◽  
Parallel Evolution ◽  
Wireless Sensor ◽  
New Techniques ◽  
Model Based ◽  
And Performance ◽  
Hardware Platforms

Advances in technology call for a parallel evolution in the software. New techniques are needed to support this dynamism, to track and guide its evolution process. This applies especially in the field of embedded systems, and certainly in Wireless Sensor Networks (WSNs), where hardware platforms and software environments change very quickly. Commonly, operating systems play a key role in the development process of any application. The most used operating system in WSNs is TinyOS, currently at its TinyOS 2.1.2 version. The evolution from TinyOS 1.x and TinyOS 2.x made the applications developed on TinyOS 1.x obsolete. In other words, these applications are not compatible out-of-the-box with TinyOS 2.x and require a porting action. In this paper, we discuss on the porting of embedded system (i.e., Wireless Sensor Networks) applications in response to operating systems’ evolution. In particular, using a model-based approach, we report the porting we did of Agilla, a Mobile-Agent Middleware (MAMW) for WSNs, on TinyOS 2.x, which we refer to as Agilla 2. We also provide a comparative analysis about the characteristics of Agilla 2 versus Agilla. The proposed Agilla 2 is compatible with TinyOS 2.x, has full capabilities and provides new features, as shown by the maintainability and performance measurement presented in this paper. An additional valuable result is the architectural modeling of Agilla and Agilla 2, missing before, which extends its documentation and improves its maintainability.

scholarly journals Host-Selected Amino Acid Changes at the Sialic Acid Binding Pocket of the Parvovirus Capsid Modulate Cell Binding Affinity and Determine Virulence

2006 ◽  
Vol 80 (3) ◽  
pp. 1563-1573 ◽  
Author(s):  
Alberto López-Bueno ◽  
Mari-Paz Rubio ◽  
Nathan Bryant ◽  
Robert McKenna ◽  
Mavis Agbandje-McKenna ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Sialic Acid ◽  
Parallel Evolution ◽  
Attachment Site ◽  
Fibroblast Cell ◽  
Scid Mice ◽  
Wild Type ◽  
Large Plaque ◽  
Capsid Sequence

ABSTRACT The role of receptor recognition in the emergence of virulent viruses was investigated in the infection of severe combined immunodeficient (SCID) mice by the apathogenic prototype strain of the parvovirus minute virus of mice (MVMp). Genetic analysis of isolated MVMp viral clones (n = 48) emerging in mice, including lethal variants, showed only one of three single changes (V325M, I362S, or K368R) in the common sequence of the two capsid proteins. As was found for the parental isolates, the constructed recombinant viruses harboring the I362S or the K368R single substitutions in the capsid sequence, or mutations at both sites, showed a large-plaque phenotype and lower avidity than the wild type for cells in the cytotoxic interaction with two permissive fibroblast cell lines in vitro and caused a lethal disease in SCID mice when inoculated by the natural oronasal route. Significantly, the productive adsorption of MVMp variants carrying any of the three mutations selected through parallel evolution in mice showed higher sensitivity to the treatment of cells by neuraminidase than that of the wild type, indicating a lower affinity of the viral particle for the sialic acid component of the receptor. Consistent with this, the X-ray crystal structure of the MVMp capsids soaked with sialic acid (N-acetyl neuraminic acid) showed the sugar allocated in the depression at the twofold axis of symmetry (termed the dimple), immediately adjacent to residues I362 and K368, which are located on the wall of the dimple, and approximately 22 Å away from V325 in a threefold-related monomer. This is the first reported crystal structure identifying an infectious receptor attachment site on a parvovirus capsid. We conclude that the affinity of the interactions of sialic-acid-containing receptors with residues at or surrounding the dimple can evolutionarily regulate parvovirus pathogenicity and adaptation to new hosts.

scholarly journals Parallel evolution of gene expression between trophic specialists despite divergent genotypes and morphologies

2018 ◽  
Vol 2 (2) ◽  
pp. 62-75 ◽  
Author(s):  
Joseph A. McGirr ◽  
Christopher H. Martin
Keyword(s):  
Gene Expression ◽  
Parallel Evolution
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