Salix hookeriana Barratt ex Hook.

https://thekeep.eiu.edu/herbarium_specimens_byname/1126/thumbnail.jp

Salix hookeriana Barratt ex Hook.

https://thekeep.eiu.edu/herbarium_specimens_byname/1126/thumbnail.jp

Salix sitchensis Sanson ex Bong.

https://thekeep.eiu.edu/herbarium_specimens_byname/2103/thumbnail.jp

Salix sitchensis Sanson ex Bong.

https://thekeep.eiu.edu/herbarium_specimens_byname/2103/thumbnail.jp

Myriophyllum hippuroides Nutt. ex Torr. & Gray

https://thekeep.eiu.edu/herbarium_specimens_byname/11059/thumbnail.jp

odoratum

Anthoxanthum odoratum Linnaeuslarge sweet vernalgrass;sweet vernalgrassflouve odorante;foin d'odeurodoratumnear Floras Creek Crossing, Highway 101, south of Bandonalong roadside and in pastures; moist sand soilsubdominanterect; flowers brownish gree

syzigachne

Beckmannia syzigachne (Steudel) FernaldAmerican sloughgrass;sloughgrass;Beckmann's grass;American shorthuskbeckmannie à écailles uniessyzigachne4 mi. S.W. of Corvallisin roadside sloughFontinalis, Downingia, Veronicaht. 0.5-1.5 m.; anthers whitis

spicata

Distichlis spicata (Linnaeus) Greenesaltgrass;seashore saltgrass;coastal saltgrass;alkali saltgrass;alkaline grass;inland saltgrassdistichlis dresséspicataTillamook Bay, along road to Cape Mears, 4 miles west of Tillamook River bridgedominant in tidewater saltmarsh, with Salicornia; wet saline mudSalicorniaextensive mat, 2-4 dm tall; flowers tinged reddish-purpl

Peptide mimics of a conformationally constrained protective epitopes of respiratory syncytial virus fusion protein

Aims: To identify peptides that mimic (mimotopes) conformational and protective epitopes of RSV fusion protein and to assess their efficacy as immunogens and potential vaccines. Material and methods: An 8-mer solid- phase (TG resin) library was screened with a neutralising and protective RSV fusion protein specific monoclonal antibodies (Mab-19). After selection of positive beads, reactive sequences were identified by microsequencing and 8- mer peptides were synthesised. Improvement of binding was analysed by amino acid replacement using the SPOTs method. Results: Mabs were not able to bind to the free and soluble peptides, nor did these peptides induce anti-RSV specific antibodies. However, several peptides re-synthesised on a TG resin (to produce de-protected 8-mer peptides linked to the resin) or as SPOTs reacted specifically. Therefore it was critical to be able to reproduce this conformation in order to use these mimotopes as immunogens and potential vaccines. Using C-terminal constrained versions of the mimotopes, strong binding of one of the Mabs to the peptides was demonstrated by surface- plasmon resonance. Immunisation of Balb/c mice with these peptide-mimics produced anti-sera that: (1) reacted specifically with RSV; (2) inhibited the binding of the Mab to the virus; (3) neutralised RSV in vitro with high titres (range: 80-640); and (4) reduce significantly the vital load in the lungs of mice challenged with RSV (P < 0.01). Conclusions: This report demonstrates for the first time that: (1) a protective epitope of the conserved RSV fusion protein can be mimicked by synthetic peptides: and (2) immunisations with these mimotopes induced specific anti-RSV neutralising antibodies and reduced vital load in vivo. These results represent a novel concept for the development of a vaccine against RSV

A peptide mimic of a protective epitope of respiratory syncytial virus selected from a combinatorial library induces virus-neutralizing antibodies and reduces viral load in vivo

Respiratory syncytial virus (RSV) is the most important cause of bronchiolitis and pneumonia in infants and young children worldwide. As yet, there is no effective vaccine against RSV infection, and previous attempts to develop a formalin-inactivated vaccine resulted in exacerbated disease in recipients subsequently exposed to the virus. In the work described here, a combinatorial solid-phase peptide library was screened with a protective monoclonal antibody (MAb 19) to identify peptide mimics (mimotopes) of a conserved and conformationally-determined epitope of RSV fusion (F) protein. Two sequences identified (S1 [HWYISKPQ] and S2 [HWYDAEVL]) reacted specifically with MAb 19 when they were presented as solid-phase peptides. Furthermore, after amino acid substitution analyses, three sequences derived from S1 (S1S [HWSISKPQ], S1K [KWYISKPQ], and S1P [HPYISKPQ]), presented as multiple antigen peptides (MAPs), also showed strong reactivity with MAb 19. The affinity constants of the binding of MAb 19, determined by surface plasmon resonance analyses, were 1.19 x 109 and 4.93 x 109 M-1 for S1 and S1S, respectively. Immunization of BALB/c mice with these mimotopes, presented as MAPs, resulted in the induction of anti-peptide antibodies that inhibited the binding of MAb 19 to RSV and neutralized viral infection in vitro, with titers equivalent to those in sera from RSV-infected animals. Following RSV challenge of S1S mimotope-immunized mice, a 98.7% reduction in the titer of virus in the lungs was observed. Furthermore, there was a greatly reduced cell infiltration in the lungs of immunized mice compared to that in controls. These results indicate the potential of peptide mimotopes to protect against RSV infection without exacerbating pulmonary pathology