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R A Lincoln

Publications and source records attributed to R A Lincoln.

12 recordsLinked to original sources
PubMed1999

PauA: a novel plasminogen activator from Streptococcus uberis.

Chromosomal DNA from two geographically distinct isolates of Streptococcus uberis was used to clone the plasminogen activator in an active form in Escherichia coli. The cloned fragments from each strain contained four potential open reading frames (ORFs). That for the plasminogen activator encoded a protein of 286 amino acids (33.4 kDa) which is cleaved between residues 25 and 26 during secretion by S. uberis. The amino acid sequence of the mature protein showed only weak homology (23.5-28%) to streptokinase. The plasminogen activator gene, pauA, in S. uberis was located between two ORFs with high homology to the DNA mismatch repair genes, hexA and hexB, and not on a DNA fragment between the genes encoding an ATP binding cassette transporter protein (abc) and a protein involved in the formation and degradation of guanosine polyphosphates (rel) as is the case for streptokinase in other streptococci.

Animals↗
PubMed1998

The interaction of Streptococcus dysgalactiae with plasmin and plasminogen.

The activation of plasminogen and the binding of plasmin by bacteria may have many effects which promote infection. The occurrence of such activities in streptococci is well documented; however, these are yet to be demonstrated for S. dysgalactiae. Consequently, the ability of this bacterium to activate mammalian plasminogen and bind either plasmin or its zymogen was investigated. Activation of bovine plasminogen was dependent on both the strain and the growth medium used for cultivation. Eighteen strain were able to activate bovine and ovine plasminogen and some of these also activated plasminogen from the horse, rabbit and pig. None activated human plasminogen and one strain (CE127) did not activate plasminogen from any source. Tricine-SDS PAGE and zymographic analysis of culture supernatants showed that bovine plasminogen was activated by four out of six strains at two locations corresponding to 16 kDa and 10 kDa. Following the growth of five strains in the presence of bovine plasminogen, all but strain CE127 bound high levels of plasmin activity. In contrast, following growth in human plasminogen none of the strains exhibited bound plasmin activity although all could bind human plasmin directly. All strains were also able to bind bovine and human plasminogen in such a way as to allow its activation by urokinase. We conclude that S. dysgalactiae is capable of activating mammalian plasminogen in a species-specific fashion and that the bacterium is also capable of binding plasmin and plasminogen with an apparent preference for bovine plasmin over human plasmin and/or plasminogen from either species.

Animals↗
PubMed1998

Characterization of the interaction of bovine plasmin with Streptococcus uberis.

The binding of plasmin to Streptococcus uberis strain 0140 J was optimal in the pH range 5.0-5.5. Plasmin binding decreased exponentially with increasing NaCl concentration (0-0.8 mol l-1), reaching a minimum at NaCl concentrations exceeding 0.55 mol l-1. Neither K+, Mg2+ nor the metal chelator EDTA had any effect on the interaction. Plasmin binding was prevented, in a concentration-dependent manner, by the amino acids lysine, arginine and epsilon-aminocaproic acid. Bound plasmin was also eluted from the bacterial cell using the same amino acids. Bound plasmin was lost from the bacterium in a time- and temperature-dependent fashion, the rate of plasmin loss increased with increasing temperature over the range 4-55 degrees C, and the elution of plasmin from live and heat-killed bacteria was similar. Cell-bound plasmin was only partially inhibited by the physiological inhibitor alpha 2-antiplasmin whereas the serine protease inhibitor aprotinin, and the active site titrant p-nitrophenyl-p-guanidiniobenzoate, inhibited the activity of the cell-bound plasmin by more than 95%.

Aminocaproates↗
PubMed1997

Streptococcus uberis acquires plasmin activity following growth in the presence of bovine plasminogen through the action of its specific plasminogen activator.

Three (0140J, C197C and EF20) out of four strains of Streptococcus uberis exhibited high levels of bound plasmin activity following growth in the presence of bovine plasminogen. The remaining strain (C197) bound considerably less plasmin following growth in the same medium. In contrast to the others, this strain was unable to activate bovine plasminogen. Following growth of strain C197 in the presence of bovine plasminogen and a source of plasminogen activator (urokinase or culture filtrate from strain 0140J) high levels of bacterially associated plasmin were detected. None of the strains was able to activate human plasminogen and only trace levels of plasmin activity were detected in association with the S. uberis following growth in the presence of human plasminogen. All strains were able to bind plasmin activity following incubation in the presence of either bovine or human plasmin. However, in each case the level of activity detected following incubation in human plasmin was approximately five-fold less than that observed following incubation with bovine plasmin. None of the strains bound detectable levels of either human or bovine plasminogen. It is concluded that activation of plasminogen is required prior to binding of plasmin by S. uberis.

Animals↗
PubMed1995

The amino acid requirements of Staphylococcus aureus isolated from cases of bovine mastitis.

The amino acid requirements of seven strains of Staphylococcus aureus isolated from cases of bovine mastitis were determined. Arginine, cystine, glycine, leucine, proline and valine were essential for the growth of all isolates. In addition, all isolates required one or more of the following: glutamic acid, histidine, isoleucine, lysine, methionine, phenylalanine, tryptophan and tyrosine.

Amino Acids↗
PubMed1983

Mortality rates in 14 Queensland Aboriginal reserve communities.

We report the results of an age standardized comparison of the mortality rates of Queenslanders and persons living in 14 Aboriginal reserves (or communities) in Queensland. The analysis distinguishes four categories of cause of death. For all causes of death, mortality rates for people living on reserves exceeded the rates for the comparable Queensland population. On some Aboriginal reserves mortality rates were substantially higher than on others. Mortality rates from infectious diseases on some reserves were 200 (Doomadgee, Woorabinda) to 300 (Lockhart River) times those which prevailed in Queensland as a whole.

Accidents↗
PubMed1983

Mortality rates in 14 Queensland Aboriginal reserve communities. Association with 10 socioenvironmental variables.

Age-standardized comparisons of mortality rates from four causes in 14 Aboriginal reserves and communities in Queensland were examined. The 14 reserves were allocated to two groups within 10 socioenvironmental variables. The findings point to an association between Queensland government Aboriginal policy, the administration of reserves, and the consequent mortality rates of the residents of these reserves.

Accidents↗