@article{dinsmore_dj o'sullivan_klaenhammer_1998, title={A leucine repeat motif in AbiA is required for resistance of Lactococcus lactis to phages representing three species.}, volume={212}, ISSN={["0378-1119"]}, DOI={10.1016/S0378-1119(98)00132-2}, abstractNote={The abiA gene encodes an abortive bacteriophage infection mechanism that can protect Lactococcus species from infection by a variety of bacteriophages including three unrelated phage species. Five heptad leucine repeats suggestive of a leucine zipper motif were identified between residues 232 and 266 in the predicted amino acid sequence of the AbiA protein. The biological role of residues in the repeats was investigated by incorporating amino acid substitutions via site-directed mutagenesis. Each mutant was tested for phage resistance against three phages, phi 31, sk1, and c2, belonging to species P335, 936, and c2, respectively. The five residues that comprise the heptad repeats were designated L234, L242, A249, L256, and L263. Three single conservative mutations of leucine to valine in positions L235, L242, and L263 and a double mutation of two leucines (L235 and L242) to valines did not affect AbiA activity on any phages tested. Non-conservative single substitutions of charged amino acids for three of the leucines (L235, L242, and L256) virtually eliminated AbiA activity on all phages tested. Substitution of the alanine residue in the third repeat (A249) with a charged residue did not affect AbiA activity. Replacement of L242 with an alanine elimination phage resistance against phi 31, but partial resistance to sk1 and c2 remained. Two single proline substitutions for leucines L242 and L263 virtually eliminated AbiA activity against all phages, indicating that the predicted alpha-helical structure of this region is important. Mutations in an adjacent region of basic amino acids had various effects on phage resistance, suggesting that these basic residues are also important for AbiA activity. This directed mutagenesis analysis of AbiA indicated that the leucine repeat structure is essential for conferring phage resistance against three species of lactococcal bacteriophages.}, number={1}, journal={GENE}, author={Dinsmore, PK and DJ O'Sullivan and Klaenhammer, TR}, year={1998}, month={May}, pages={5–11} }
 @article{dinsmore_klaenhammer_1997, title={Molecular characterization of a genomic region in a Lactococcus bacteriophage that is involved in its sensitivity to the phage defense mechanism AbiA}, volume={179}, ISSN={["0021-9193"]}, DOI={10.1128/jb.179.9.2949-2957.1997}, abstractNote={A spontaneous mutant of the lactococcal phage phi31 that is insensitive to the phage defense mechanism AbiA was characterized in an effort to identify the phage factor(s) involved in sensitivity of phi31 to AbiA. A point mutation was localized in the genome of the AbiA-insensitive phage (phi31A) by heteroduplex analysis of a 9-kb region. The mutation (G to T) was within a 738-bp open reading frame (ORF245) and resulted in an arginine-to-leucine change in the predicted amino acid sequence of the protein. The mutant phi31A-ORF245 reduced the sensitivity of phi31 to AbiA when present in trans, indicating that the mutation in ORF245 is responsible for the AbiA insensitivity of phi31A. Transcription of ORF245 occurs early in the phage infection cycles of phi31 and phi31A and is unaffected by AbiA. Expansion of the phi31 sequence revealed ORF169 (immediately upstream of ORF245) and ORF71 (which ends 84 bp upstream of ORF169). Two inverted repeats lie within the 84-bp region between ORF71 and ORF169. Sequence analysis of an independently isolated AbiA-insensitive phage, phi31B, identified a mutation (G to A) in one of the inverted repeats. A 118-bp fragment from phi31, encompassing the 84-bp region between ORF71 and ORF169, eliminates AbiA activity against phi31 when present in trans, establishing a relationship between AbiA and this fragment. The study of this region of phage phi31 has identified an open reading frame (ORF245) and a 118-bp DNA fragment that interact with AbiA and are likely to be involved in the sensitivity of this phage to AbiA.}, number={9}, journal={JOURNAL OF BACTERIOLOGY}, author={Dinsmore, PK and Klaenhammer, TR}, year={1997}, month={May}, pages={2949–2957} }
 @inbook{monks_goode_dinsmore_dewey_1997, title={Phosphatidylcholine biosynthesis in soybeans: The cloning and characterization of genes encoding enzymes of the nucleotide pathway}, DOI={10.1007/978-94-017-2662-7_35}, booktitle={Physiology, biochemistry, and molecular biology of plant lipids}, publisher={Dordrecht; Boston: Kluwer Academic}, author={Monks, D. E. and Goode, J. H. and Dinsmore, P. K. and Dewey, R. E.}, editor={J. P. Williams, M. U. Khan and Lem, N. W.Editors}, year={1997}, pages={110–112} }
 @misc{dinsmore_klaenhammer_1995, title={Bacteriophage resistance in Lactococcus}, volume={4}, ISSN={["1073-6085"]}, DOI={10.1007/BF02779022}, abstractNote={Lactic acid bacteria are industrial microorganisms used in many food fermentations. Lactococcus species are susceptible to bacteriophage infections that may result in slowed or failed fermentations. A substantial amount of research has focused on characterizing natural mechanisms by which bacterial cells defend themselves against phage. Numerous natural phage defense mechanisms have been identified and studied, and recent efforts have improved phage resistance by using molecular techniques. The study of how phages overcome these resistance mechanisms is also an important objective. New strategies to minimize the presence, virulence, and evolution of phage are being developed and are likely to be applied industrially.}, number={3}, journal={MOLECULAR BIOTECHNOLOGY}, author={Dinsmore, PK and Klaenhammer, TR}, year={1995}, month={Dec}, pages={297–314} }
 @article{dinsmore_klaenhammer_1994, title={Phenotypic consequences of altering the copy number of abiA, a gene responsible for aborting bacteriophage infections in Lactococcus lactis}, volume={60}, number={4}, journal={Applied and Environmental Microbiology}, author={Dinsmore, P. K. and Klaenhammer, T. R.}, year={1994}, pages={1129} }
 @article{dinsmore_romero_klaenhammer_1993, title={INSERTIONAL MUTAGENESIS IN LACTOCOCCUS-LACTIS SUBSP LACTIS MEDIATED BY IS946}, volume={107}, ISSN={["0378-1097"]}, DOI={10.1016/0378-1097(93)90351-2}, number={1}, journal={FEMS MICROBIOLOGY LETTERS}, author={DINSMORE, PK and ROMERO, DA and KLAENHAMMER, TR}, year={1993}, month={Feb}, pages={43–48} }
 @article{dinsmore_klaenhammer_1992, title={IS946-mediated integration of an abortive bacteriophage resistance gene (hsp) into the Lactococcus lactis subsp. lactis genome}, volume={75}, journal={Journal of Dairy Science}, author={Dinsmore, P. K. and Klaenhammer, T. R.}, year={1992}, pages={113} }
 @article{dinsmore_romero_klaenhammer_1991, title={Insertional mutagenesis in Lactococcus lactis subsp. lactis mediated by IS946}, volume={74}, journal={Journal of Dairy Science}, author={Dinsmore, P. K. and Romero, D. A. and Klaenhammer, T. R.}, year={1991}, pages={83} }