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Results for “selection pressure”

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At least 199 records · Page 11Linked to original sources
PubMed1990

A mutant neomycin phosphotransferase II gene reduces the resistance of transformants to antibiotic selection pressure.

The neo (neomycin-resistance) gene of transposon Tn5 encodes the enzyme neomycin phosphotransferase II (EC 2.7.1.95), which confers resistance to various aminoglycoside antibiotics, including kanamycin and G418. The gene is widely used as a selectable marker in the transformation of organisms as diverse as bacteria, yeast, plants, and animals. We found a mutation that involves a glutamic to aspartic acid conversion at residue 182 in the protein encoded by the chimeric neomycin phosphotransferase II genes of several commonly used transformation vectors. The mutation substantially reduces phosphotransferase activity but does not appear to affect the stability of the neomycin phosphotransferase II mRNA or protein. Plants and bacteria transformed with the mutant gene are less resistant to antibiotics than those transformed with the normal gene. A simple restriction endonuclease digestion distinguishes between the mutant and the normal gene.

Anti-Bacterial Agents↗
PubMed1990

Effect of selection pressure for thiabendazole resistance on fitness of Haemonchus contortus in sheep.

A strain of Haemonchus contortus showing moderate levels of resistance to thiabendazole (TBZ) (egg hatch assay LC50 2.1 microM) was subjected, in alternating sequence, to 5 in vitro and 4 in vivo selections with TBZ. This resulted in a significant increase in resistance (egg hatch assay LC50 2.8 microM). The isolates obtained after each combined in vitro and in vivo selection were compared in terms of egg hatch assay, establishment, net egg output, per capita egg output and degree of pathology caused in infected hosts. The increase in resistance was accompanied by a significant increase in larval establishment in sheep (22.8-39.2%) and was associated with more severe pathology, higher egg count and worm recovery 3 months post-infection. The resistant strains were also compared with a TBZ-susceptible strain (egg hatch assay LC50 1.0 microM). The TBZ-susceptible strain had the highest net egg output, it caused the most severe pathology and it resulted in higher worm recovery than any of the TBZ-resistant strains, although the most resistant strain was very similar to the TBZ-susceptible strain. Neither the per capita egg output nor biological features of the free-living stages were significantly affected by the degree of resistance. The implications of these observations for anthelmintic use and for management of nematode anthelmintic resistance in the field are discussed.

Animals↗
PubMed1984

Antibiotic selection pressure resulting in multiple antibiotic resistance and localization of resistance determinants to conjugative plasmids in streptococci.

The plasmid content, antibiotic susceptibilities, and biochemical traits of fecal streptococci isolated from pigs during a tylosin feeding experiment were analyzed. The presence of tylosin in the feed did not select for a particular streptococcal strain or biochemical type but did select for multiple antibiotic resistance. A DNA probe obtained from Escherichia coli and containing a cloned macrolide-lincosamide-streptogramin B (MLS) resistance determinant from a streptococcal strain of human origin hybridized primarily to large plasmids among MLS-resistant streptococci from antibiotic-fed pigs. Patterns of hybridization were similar among MLS-resistant clinical isolates from human infections and isolates from other antibiotic-fed animals. The results of mating experiments indicated that tylosin selected for localization of the MLS determinants to large conjugative plasmids. These data established (1) a strong sequence homology between MLS resistance genes in isolates from humans and those from farm animals and (2) an increased potential for dissemination of MLS resistance as a consequence of tylosin feeding.

Animal Feed↗
PubMed2004

Bigger is not always better: conflicting selective pressures on seed size in Quercus ilex.

Most theoretical treatments of the evolutionary ecology of offspring size assume a simple and direct effect of investment per offspring on offspring fitness. In this paper I experimentally determine the relationship between seed mass and several main fitness components of the oak Quercus ilex, to estimate phenotypic selection acting on seed mass during the early life cycle and to discover any potential selective conflicts occurring between different stages from dispersal to establishment. I found a positive effect of acorn size on most fitness components related to seedling establishment. Large size increased germination rate and seedling survival, accelerated germination timing, and enhanced seedling growth. Nevertheless, there was also a direct negative effect of acorn size on survival to predation, because large acorns were highly preferred by the main postdispersal seed predators at the study site, wild boars and wood mice. Because of the low probability of escape from predation, the fitness of large acorns estimated on this component was significantly lower than the fitness of smaller acorns. Therefore, seed size affected fitness in two different ways, yielding opposing and conflicting selective forces. These findings suggest that the general assumption that offspring fitness is a fixed positive function of seed size needs to be reconsidered for some systems. The existence of conflicting selection might explain the occurrence of an optimal seed size in some plant species without invoking a seed number-size trade-off.

Phenotype↗
PubMed2000

Structural adaptation to selective pressure for altered ligand specificity in the Pseudomonas aeruginosa amide receptor, amiC.

The AmiC protein in Pseudomonas aeruginosa is the negative regulator and ligand receptor for an amide-inducible aliphatic amidase operon. In the wild-type PAC1 strain, amidase expression is induced by acetamide or lactamide, but not by butyramide. A mutant strain of P. aeruginosa, PAC181, was selected for its sensitivity to induction by butyramide. The molecular basis for the butyramide inducible phenotype of P.aeruginosa PAC181 has now been determined, and results from a Thr-->Asn mutation at position 106 in PAC181-AmiC. In the wild-type PAC1-AmiC protein this residue forms part of the side wall of the amide-binding pocket but does not interact with the acetamide ligand directly. In the crystal structure of PAC181-AmiC complexed with butyramide, the Thr-->Asn mutation increases the size of the ligand binding site such that the mutant protein is able to close into its 'on' configuration even in the presence of butyramide. Although the mutation allows butyramide to be recognized as an inducer of amidase expression, the mutation is structurally sub-optimal, and produces a significant decrease in the stability of the mutant protein.

Adaptation, Biological↗