Traveltime, unit-concentration, longitudinal-dispersion, and reaeration characteristics of upstream reaches of the Yampa and Little Snake Rivers, Colorado and Wyoming /

Mode of access: Internet.

Remarks on the uses of some of the bazaar medicines and common medical plants of India : with a full index of diseases, indicating their treatment by these and other agents procurable throughout India : to which are added directions for treatment in cases of drowning, snake-bites &c. /

Reprint. Originally published: 5th ed. London, J.&A. Churchill, 1897.

Chemical and physical data for disposal wells, Eastern Snake River Plain, Idaho /

Bibliography: leaves 30-31.

The wild and scenic Snake River : Hells Canyon National Recreation Area.

Shipping list no.: 94-0263-P.

Seasonal development and yield of native plants on the upper Snake River Plains and their relation to certain climatic factors /

Issued also in microfilm form, as thesis, University of Minnesota, under title: Seasonal development and yield of native plants on the upper Snake River Plains of Idaho and their relation to climatic factors, especially precipitation and temperature.

Hells Canyon-Snake National River. Hearings, Ninety-second Congress, first session, on S. 717 and S. 448 ... September 16, 17, and 30, 1971

Includes bibliographical references

Snake river, Oreg., Wash., and Idaho : hearings before the Committee on Rivers and Harbors, House of Representatives, Seventy-seventy Congress, first session on the subject of the improvement of the Snake river, Oreg., Wash., and Idaho. September 22, and October 15, 1941.

Mode of access: Internet.

Snake-bite, and other stories,

- Snake-bite.- The lost faith.- The Hindu.- The lighted candles.- The nomad.- The two fears.

Comparative osteology of the snake families Typhlopidae and Leptotyphlopidae.

Bibliography: p. 104-106.

Craig District (White River, Kremmling, and Little Snake resource areas) : final wilderness environmental impact statement : Grand, Jackson, Moffat, and Rio Blanco counties, Colorado; Daggett and Uintah counties, Utah /

"November 1990"--Cover.

Negative regulation of prophenoloxidase (proPO) activation by a clip-domain serine proteinase homolog (SPH) from endoparasitoid venom

Most parasitic wasps inject maternal factors into the host hemocoel to suppress the host immune system and ensure successful development of their progeny. Melanization is one of the insect defence mechanisms against intruding pathogens or parasites. We previously isolated from the venom of Cotesia rubecula a 50 kDa protein that blocked melanization in the hemolymph of its host, Pieris rapae [Insect Biochem. Mol. Biol. 33 (2003) 1017]. This protein, designated Vn50, is a serine proteinase homolog (SPH) containing an amino-terminal clip domain. In this work, we demonstrated that recombinant Vn50 bound P. rapae hemolymph components that were recognized by antisera to Tenebrio molitor prophenoloxidase (proPO) and Manduca sexta proPO-activating proteinase (PAP). Vn50 is stable in the host hemolymph-it remained intact for at least 72 It after parasitization. Using M. sexta as a model system, we found that Vn50 efficiently down-regulated proPO activation mediated by M. sexta PAP-1, SPH-1, and SPH-2. Vn50 did not inhibit active phenoloxidase (PO) or PAP-1, but it significantly reduced the proteolysis of proPO. If recombinant Vn50 binds P. rapae proPO and PAP (as suggested by the antibody reactions), it is likely that the molecular interactions among M. sexta proPO, PAP-1, and SPHs were impaired by this venom protein. A similar strategy might be employed by C rubecula to negatively impact the proPO activation reaction in its natural host. (C) 2004 Elsevier Ltd. All rights reserved.

A novel venom peptide from an endoparasitoid wasp is required for expression of polydnavirus genes in host hemocytes

Maternal factors introduced into host insects by endoparasitoid wasps are usually essential for successful parasitism. This includes polydnaviruses (PDVs) that are produced in the reproductive organ of female hymenopteran endoparasitoids and are injected, together with venom proteins, into the host hemocoel at oviposition. Inside the host, PDVs enter various tissue cells and hemocytes where viral genes are expressed, leading to developmental and physiological alterations in the host, including the suppression of the host immune system. Although several studies have shown that some PDVs are only effective when accompanied by venom proteins, there is no report of an active venom ingredient(s) facilitating PDV infection and/or gene expression. In this study, we describe a novel peptide (Vn1.5) isolated from Cotesia rubecula venom that is required for the expression of C. rubecula bracoviruses (CrBVs) in host hemocytes (Pieris rapae), although it is not essential for CrBV entry into host cells. The peptide consists of 14 amino acids with a molecular mass of 1598 Da. In the absence of Vn1.5 or total venom proteins, CrBV genes are not expressed in host cells and did not cause inactivation of host hemocytes.