Soybeans Thomas Alan Orr Analysis Essay

Two Poems by Thomas Alan Orr: "Doppelganger" and "Moose Into Osprey"

Thomas Alan Orr is a native New Englander who has lived in Indiana for the past forty years. He lives on a small farm in Shelby County. He raises and shows Flemish Giant rabbits. His most recent book,Tongue to the Anvil, was published in 2014 by Restoration Press. His poetry has been featured in Good Poems, edited by Garrison Keillor, and has appeared in numerous journals.







Doppelganger


That night the trestle buckled, spilling tanker cars
into the Big Blue River, Schultz the engineer cried out
to God in anguish, while Mae and Buzz made love
in a rented room above the village bar, their passion
fending off this dark convergence of steel and steel.

Schultz, in the forward cab, hit the air horn a quarter mile
before the crossing – two long blasts, a short, a long –
the universal warning that rang against
the grain elevator and bounced off the window
above the bar, blending with the fervid cries of love.

The big locomotive – a Seventy Mac with a drone –
pulled hard one hundred cars through fog.
Schultz swore he saw a light ahead, beyond the trestle,
something or someone on the tracks – yes –
a child swinging a lantern, a child who looked like Schultz.

Ah, Schultz – occasional Lutheran, twice divorced,
who longed for the child he never had, chasing the rails
these thirty years, town to town, stepping off at times
for two fingers of bourbon and a Lucky Strike –
had seen it before, the figure on the tracks – dear God!

Long past the time of flagmen with lanterns in the dark,
he was haunted by what he dared not name – memory or ghost
or the rail mirage that visits every weary engineer
immersed in the roar of a speeding locomotive –
the honest dread of his own mortal soul.

At the moment the train uncoupled on the trestle,
that coupling in a rented room above the bar
made a child not yet known, less loved
and less desired than the longing in the heart
of Schultz the engineer, on whom be grace and peace.



Moose Into Osprey 

Perhaps it was the taste of salt
In dusky air, or early moonlight,
Or the tide that rose so quietly.
The sound of turning stones beneath
Each wave was sharp and clear as dice
Tossed lightly up against a wall.

The last of the lobster boats chugged
Into the harbor toward the slip.
A wreath of diesel vapor curled
Above the pines along the shore,
Their boughs caressing rocky beach
With quiet murmurs, like a chant.

Without a warning, from the woods
There came a crash, a bellowed call.
It was a giant bull. He strode
The beach with royal swagger, paused.
A fog set in. He looked out toward
The island and began to swim.

His massive crown like driftwood bobbed.
Then fog obscured him as a flash
Of white disturbed the air.
A sudden rush of wings rose up,
Diaphanous and ghostly too,
A vision to unsettle sense.

The osprey hovered, wings spread wide,
As if to shed the final trace
Of fur and antler in the fog.
He disappeared. A whistling note
Rang like a vesper bell. The sea
Was still, the world caught in her spell.


Thomas Alan Orr

1. Steinmann P., Keiser J., Bos R., Tanner M., Utzinger J. Schistosomiasis and water resources development: systematic review, meta-analysis, and estimates of people at risk. Lancet Infect. Dis. 2006;6:411–425.[PubMed]

2. Utzinger J., Becker S.L., Knopp S., Blum J., Neumayr A.L., Keiser J., Hatz C.F. Neglected tropical diseases: diagnosis, clinical management, treatment and control. Swiss Med. Wkly. 2012;142:w13727.[PubMed]

3. Chitsulo L., Engels D., Montresor A., Savioli L. The global status of schistosomiasis and its control. Acta Trop. 2000;77:41–51.[PubMed]

4. Colley D.G., Bustinduy A.L., Secor W.E., King C.H. Human schistosomiasis. Lancet. 2014;383:2253–2264.[PubMed]

5. Cioli D., Pica-Mattoccia L., Basso A., Guidi A. Schistosomiasis control: praziquantel forever? Mol. Biochem. Parasitol. 2014;195:23–29.[PubMed]

6. Greenberg R.M. Are Ca2+ channels targets of praziquantel action? Int. J. Parasitol. 2005;35:1–9.[PubMed]

7. Doenhoff M.J., Cioli D., Utzinger J. Praziquantel: mechanisms of action, resistance and new derivatives for schistosomiasis. Curr. Opin. Infect. Dis. 2008;21:659–667.[PubMed]

8. Angelucci F., Basso A., Bellelli A., Brunori M., Pica Mattoccia L., Valle C. The anti-schistosomal drug praziquantel is an adenosine antagonist. Parasitology. 2007;134:1215–1221.[PubMed]

9. Gnanasekar M., Salunkhe A.M., Mallia A.K., He Y.X., Kalyanasundaram R. Praziquantel affects the regulatory myosin light chain of Schistosoma mansoni. Antimicrob. Agents Chemother. 2009;53:1054–1060.[PubMed]

10. Wang W., Wang L., Liang Y.S. Susceptibility or resistance of praziquantel in human schistosomiasis: a review. Parasitol. Res. 2012;111:1871–1877.[PubMed]

11. Fallon P.G., Doenhoff M.J. Drug-resistant schistosomiasis: resistance to praziquantel and oxamniquine induced in Schistosoma mansoni in mice is drug specific. Am. J. Trop. Med. Hyg. 1994;51:83–88.[PubMed]

12. Pica-Mattoccia L., Dias L.C., Moroni R., Cioli D. Schistosoma mansoni: genetic complementation analysis shows that two independent hycanthone/oxamniquine-resistant strains are mutated in the same gene. Exp. Parasitol. 1993;77:445–449.[PubMed]

13. Brennan G.P., Fairweather I., Trudgett A., Hoey E., McCoy, McConville M., Meaney M., Robinson M., McFerran N., Ryan L., Lanusse C., Mottier L., Alvarez L., Solana H., Virkel G., Brophy P.M. Understanding triclabendazole resistance. Exp. Mol. Pathol. 2007;82:104–109.[PubMed]

14. Jabbar A., Iqbal Z., Kerboeuf D., Muhammad G., Khan M.N., Afaq M. Anthelmintic resistance: the state of play revisited. Life Sci. 2006;79:2413–2431.[PubMed]

15. Berridge M.J., Lipp P., Bootman M.D. The versatility and universality of calcium signalling. Nat. Rev. Mol. Cell. Biol. 2000;1:11–21.[PubMed]

16. Chin D., Means A.R. Calmodulin: a prototypical calcium sensor. Trends Cell. Biol. 2000;10:322–328.[PubMed]

17. Gifford J.L., Walsh M.P., Vogel H.J. Structures and metal-ion-binding properties of the Ca2+-binding helix-loop-helix EF-hand motifs. Biochem. J. 2007;405:199–221.[PubMed]

18. Hoffmann K.F., Strand M. Molecular characterization of a 20.8-kDa Schistosoma mansoni antigen. Sequence similarity to tegumental associated antigens and dynein light chains. J. Biol. Chem. 1997;272:14509–14515.[PubMed]

19. Jeffs S.A., Hagan P., Allen R., Correa-Oliveira R., Smithers S.R., Simpson A.J. Molecular cloning and characterisation of the 22-kilodalton adult Schistosoma mansoni antigen recognised by antibodies from mice protectively vaccinated with isolated tegumental surface membranes. Mol. Biochem. Parasitol. 1991;46:159–167.[PubMed]

20. Francis P., Bickle Q. Cloning of a 21.7-kDa vaccine-dominant antigen gene of Schistosoma mansoni reveals an EF hand-like motif. Mol. Biochem. Parasitol. 1992;50:215–224.[PubMed]

21. Mohamed M.M., Shalaby K.A., LoVerde P.T., Karim A.M. Characterization of Sm20.8, a member of a family of schistosome tegumental antigens. Mol. Biochem. Parasitol. 1998;96:15–25.[PubMed]

22. Lopes D.O., Paiva L.F., Martins M.A., Cardoso F.C., Rajao M.A., Pinho J.M., Caliari M.V., Correa-Oliveira R., Mello S.M., Leite L.C., Oliveira S.C. Sm21.6 a novel EF-hand family protein member located on the surface of Schistosoma mansoni adult worm that failed to induce protection against challenge infection but reduced liver pathology. Vaccine. 2009;27:4127–4135.[PubMed]

23. Fitzsimmons C.M., Jones F.M., Stearn A., Chalmers I.W., Hoffmann K.F., Wawrzyniak J., Wilson S., Kabatereine N.B., Dunne D.W. The Schistosoma mansoni tegumental-allergen-like (TAL) protein family: influence of developmental expression on human IgE responses. PLoS Negl. Trop. Dis. 2012;6:e1593.[PubMed]

24. Waine G.J., Becker M.M., Scott J.C., Kalinna B.H., Yang W., McManus D.P. Purification of a recombinant Schistosoma japonicum antigen homologous to the 22-kDa membrane-associated antigen of S. mansoni, a putative vaccine candidate against schistosomiasis. Gene. 1994;142:259–263.[PubMed]

25. Xu J., Ren Y., Xu X., Chen J., Li Y., Gan W., Zhang Z., Zhan H., Hu X. Schistosoma japonicum tegumental protein 20.8, role in reproduction through its calcium binding ability. Parasitol. Res. 2014;113:491–497.[PubMed]

26. Fitzsimmons C.M., Stewart T.J., Hoffmann K.F., Grogan J.L., Yazdanbakhsh M., Dunne D.W. Human IgE response to the Schistosoma haematobium 22.6 kDa antigen. Parasite Immunol. 2004;26:371–376.[PubMed]

27. Zhang Z., Xu H., Gan W., Zeng S., Hu X. Schistosoma japonicum calcium-binding tegumental protein SjTP22.4 immunization confers praziquantel schistosomulumicide and antifecundity effect in mice. Vaccine. 2012;30:5141–5150.[PubMed]

28. Vichasri-Grams S., Subpipattana P., Sobhon P., Viyanant V., Grams R. An analysis of the calcium-binding protein 1 of Fasciola gigantica with a comparison to its homologs in the phylum Platyhelminthes. Mol. Biochem. Parasitol. 2006;146:10–23.[PubMed]

29. Subpipattana P., Grams R., Vichasri-Grams S. Analysis of a calcium-binding EF-hand protein family in Fasciola gigantica. Exp..Parasitol. 2012;130:364–373.[PubMed]

30. Orr R., Kinkead R., Newman R., Anderson L., Hoey E.M., Trudgett A., Timson D.J. FhCaBP4: a Fasciola hepatica calcium-binding protein with EF-hand and dynein light chain domains. Parasitol. Res. 2012;111:1707–1713.[PubMed]

31. Banford S., Drysdale O., Hoey E.M., Trudgett A., Timson D.J. FhCaBP3: a Fasciola hepatica calcium binding protein with EF-hand and dynein light chain domains. Biochimie. 2013;95:751–758.[PubMed]

32. Ruiz de Eguino A.D., Machin A., Casais R., Castro A.M., Boga J.A., Martin-Alonso J.M., Parra F. Cloning and expression in Escherichia coli of a Fasciola hepatica gene encoding a calcium-binding protein. Mol. Biochem. Parasitol. 1999;101:13–21.[PubMed]

33. Kim Y.J., Yoo W.G., Lee M.R., Kim D.W., Lee W.J., Kang J.M., Na B.K., Ju J.W. Identification and characterization of a novel 21.6-kDa tegumental protein from Clonorchis sinensis. Parasitol. Res. 2012;110:2061–2066.[PubMed]

34. Senawong G., Laha T., Loukas A., Brindley P.J., Sripa B. Cloning, expression, and characterization of a novel Opisthorchis viverrini calcium-binding EF-hand protein. Parasitol. Int. 2012;61:94–100.[PubMed]

35. Fitzsimmons C.M., McBeath R., Joseph S., Jones F.M., Walter K., Hoffmann K.F., Kariuki H.C., Mwatha J.K., Kimani G., Kabatereine N.B., Vennervald B.J., Ouma J.H., Dunne D.W. Factors affecting human IgE and IgG responses to allergen-like Schistosoma mansoni antigens: molecular structure and patterns of in vivo exposure. Int. Arch. Allergy Immunol. 2007;142:40–50.[PubMed]

36. Santiago M.L., Hafalla J.C., Kurtis J.D., Aligui G.L., Wiest P.M., Olveda R.M., Olds G.R., Dunne D.W., Ramirez B.L. Identification of the Schistosoma japonicum 22.6-kDa antigen as a major target of the human IgE response: similarity of IgE-binding epitopes to allergen peptides. Int. Arch. Allergy Immunol. 1998;117:94–104.[PubMed]

37. Pacifico L.G., Fonseca C.T., Chiari L., Oliveira S.C. Immunization with Schistosoma mansoni 22.6 kDa antigen induces partial protection against experimental infection in a recombinant protein form but not as DNA vaccine. Immunobiology. 2006;211:97–104.[PubMed]

38. Lin Y.L., He S. Sm22.6 antigen is an inhibitor to human thrombin. Mol. Biochem. Parasitol. 2006;147:95–100.[PubMed]

39. Kelley L.A., Sternberg M.J. Protein structure prediction on the Web: a case study using the Phyre server. Nat. Protoc. 2009;4:363–371.[PubMed]

40. Krieger E., Joo K., Lee J., Lee J., Raman S., Thompson J., Tyka M., Baker D., Karplus K. Improving physical realism, stereochemistry, and side-chain accuracy in homology modeling: four approaches that performed well in CASP8. Proteins. 2009;77(Suppl 9):114–122.[PubMed]

41. Ishida H., Huang H., Yamniuk A.P., Takaya Y., Vogel H.J. The solution structures of two soybean calmodulin isoforms provide a structural basis for their selective target activation properties. J. Biol. Chem. 2008;283:14619–14628.[PubMed]

42. Akerboom J., Carreras Calderon N., Tian L., Wabnig S., Prigge M., Tolo J., Gordus A., Orger M.B., Severi K.E., Macklin J.J., Patel R., Pulver S.R., Wardill T.J., Fischer E., Schuler C., Chen T.W., Sarkisyan K.S., Marvin J.S., Bargmann C.I., Kim D.S., Kugler S., Lagnado L., Hegemann P., Gottschalk A., Schreiter E.R., Looger L.L. Genetically encoded calcium indicators for multi-color neural activity imaging and combination with optogenetics. Front. Mol. Neurosci. 2013;6:2.[PubMed]

43. McLellan T. Electrophoresis buffers for polyacrylamide gels at various pH. Anal. Biochem. 1982;126:94–99.[PubMed]

44. Zinsser V.L., Hoey E.M., Trudgett A., Timson D.J. Biochemical characterisation of triose phosphate isomerase from the liver fluke Fasciola hepatica. Biochimie. 2013;95:2182–2189.[PubMed]

45. Megarity C.F., Huang M., Warnock C., Timson D.J. The role of the active site residues in human galactokinase: Implications for the mechanisms of GHMP kinases. Bioorg. Chem. 2011;39:120–126.[PubMed]

46. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976;72:248–254.[PubMed]

47. Costa M.A., Rodrigues F.T., Chagas B.C., Rezende C.M., Goes A.M., Nagem R.A. Preliminary crystallographic studies of a Schistosoma mansoni antigen (Sm21.7) dynein light-chain (DLC) domain. Acta Crystallogr. F. Struct. Biol. Commun. 2014;70:803–807.[PubMed]

48. Babu Y.S., Sack J.S., Greenhough T.J., Bugg C.E., Means A.R., Cook W.J. Three-dimensional structure of calmodulin. Nature. 1985;315:37–40.[PubMed]

49. Ericsson U.B., Hallberg B.M., Detitta G.T., Dekker N., Nordlund P. Thermofluor-based high-throughput stability optimization of proteins for structural studies. Anal. Biochem. 2006;357:289–298.[PubMed]

50. Cook W.J., Walter L.J., Walter M.R. Drug binding by calmodulin: crystal structure of a calmodulin-trifluoperazine complex. Biochemistry. 1994;33:15259–15265.[PubMed]

51. Osawa M., Swindells M.B., Tanikawa J., Tanaka T., Mase T., Furuya T., Ikura M. Solution structure of calmodulin-W-7 complex: the basis of diversity in molecular recognition. J. Mol. Biol. 1998;276:165–176.[PubMed]

52. Tanaka T., Ohmura T., Hidaka H. Calmodulin antagonists' binding sites on calmodulin. Pharmacology. 1983;26:249–257.[PubMed]

53. Gonzalez-Andrade M., Del Valle P., Macias-Rubalcava M.L., Sosa-Peinado A., Del Carmen Gonzalez M., Mata R. Calmodulin inhibitors from Aspergillus stromatoides. Chem. Biodivers. 2013;10:328–337.[PubMed]

54. Humar M., Pischke S.E., Loop T., Hoetzel A., Schmidt R., Klaas C., Pahl H.L., Geiger K.K., Pannen B.H. Barbiturates directly inhibit the calmodulin/calcineurin complex: a novel mechanism of inhibition of nuclear factor of activated T cells. Mol. Pharmacol. 2004;65:350–361.[PubMed]

55. Russell S.L., McFerran N.V., Hoey E.M., Trudgett A., Timson D.J. Characterisation of two calmodulin-like proteins from the liver fluke, Fasciola hepatica. Biol. Chem. 2007;388:593–599.[PubMed]

56. Russell S.L., McFerran N.V., Moore C.M., Tsang Y., Glass P., Hoey E.M., Trudgett A., Timson D.J. A novel calmodulin-like protein from the liver fluke, Fasciola hepatica. Biochimie. 2012;94:2398–2406.[PubMed]

57. Cooper A., Nutley M.A., Wadood A. 2001. Differential Scanning Microcalorimetry.

58. Liang J., Jaffrey S.R., Guo W., Snyder S.H., Clardy J. Structure of the PIN/LC8 dimer with a bound peptide. Nat. Struct. Biol. 1999;6:735–740.[PubMed]

59. Barbar E., Kleinman B., Imhoff D., Li M., Hays T.S., Hare M. Dimerization and folding of LC8, a highly conserved light chain of cytoplasmic dynein. Biochemistry. 2001;40:1596–1605.[PubMed]

60. Lafitte D., Heck A.J., Hill T.J., Jumel K., Harding S.E., Derrick P.J. Evidence of noncovalent dimerization of calmodulin. Eur. J. Biochem. 1999;261:337–344.[PubMed]

61. Streicher W.W., Lopez M.M., Makhatadze G.I. Modulation of quaternary structure of S100 proteins by calcium ions. Biophys. Chem. 2010;151:181–186.[PubMed]

62. Timson D.J., Reece R.J. Functional analysis of disease-causing mutations in human galactokinase. Eur. J. Biochem. 2003;270:1767–1774.[PubMed]

63. Ben-Johny M., Yue D.T. Calmodulin regulation (calmodulation) of voltage-gated calcium channels. J. Gen. Physiol. 2014;143:679–692.[PubMed]

64. Simms B.A., Souza I.A., Zamponi G.W. A novel calmodulin site in the Cav1.2 N-terminus regulates calcium-dependent inactivation. Pflugers Arch. 2014;466:1793–1803.[PubMed]

65. Minor D.L., Jr., Findeisen F. Progress in the structural understanding of voltage-gated calcium channel (CaV) function and modulation. Channels (Austin) 2010;4:459–474.[PubMed]

66. Coles G.C. The effect of praziquantel on Schistosoma mansoni. J. Helminthol. 1979;53:31–33.[PubMed]

0 comments

Leave a Reply

Your email address will not be published. Required fields are marked *