A Theorem on Matroid Homomorphism

This note generalizes a result contained in a previous paper [ J. Sanders, Circuit preserving edge maps II, J. Combin. Theory Ser. B 42 (1987), 146-155].Comment: 5 pages, 0 figure

LC-MS/MS spectral counts of functionally interesting proteins identified in sporocyst/sporozoite fractions of <i>Toxoplasma gondii</i> oocysts – SRS family proteins.

<p>LC-MS/MS spectral counts of functionally interesting proteins identified in sporocyst/sporozoite fractions of <i>Toxoplasma gondii</i> oocysts – SRS family proteins.</p

LC-MS/MS spectral counts of functionally interesting proteins identified in sporocyst/sporozoite fractions of <i>Toxoplasma gondii</i> oocysts – other proteins of interest.

<p>LC-MS/MS spectral counts of functionally interesting proteins identified in sporocyst/sporozoite fractions of <i>Toxoplasma gondii</i> oocysts – other proteins of interest.</p

Flow chart showing experimental design for sample collection and processing of <i>Toxoplasma gondii</i> oocysts.

<p>Flow chart showing experimental design for sample collection and processing of <i>Toxoplasma gondii</i> oocysts.</p

Summary of LC-MS/MS spectral counts and protein identification in sporocyst/sporozoite and oocyst wall fractions of <i>Toxoplasma gondii</i> oocysts.

<p>Summary of LC-MS/MS spectral counts and protein identification in sporocyst/sporozoite and oocyst wall fractions of <i>Toxoplasma gondii</i> oocysts.</p

LC-MS/MS spectral counts of abundantly detected proteins in <i>Toxoplasma gondii</i> sporocyst/sporozoite fractions.

<p>LC-MS/MS spectral counts of abundantly detected proteins in <i>Toxoplasma gondii</i> sporocyst/sporozoite fractions.</p

LC-MS/MS spectral counts of most abundantly detected proteins in <i>Toxoplasma gondii</i> oocyst wall fractions showing spectral counts (% of all spectral counts) in each experimental group.

<p>LC-MS/MS spectral counts of most abundantly detected proteins in <i>Toxoplasma gondii</i> oocyst wall fractions showing spectral counts (% of all spectral counts) in each experimental group.</p

LC-MS/MS spectral counts of tyrosine-rich (>5%) and putative oocyst wall proteins identified in sporocyst/sporozoite and wall fractions of <i>Toxoplasma gondii</i> oocysts.

<p>LC-MS/MS spectral counts of tyrosine-rich (>5%) and putative oocyst wall proteins identified in sporocyst/sporozoite and wall fractions of <i>Toxoplasma gondii</i> oocysts.</p

The <i>Toxoplasma gondii</i> oocyst and sporocyst walls are autofluorescent under UV excitation.

<p>A. Epifluorescent and bright field images of intact, mature oocysts 10 days after exposure to maturing conditions showing intact oocysts (“oocyst”), isolated sporocysts (“sporocyst”), and isolated oocyst walls (“wall”), the latter two fractions being derived from mature oocysts by glass bead disruption and gradient centrifugation as detailed in the <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0029955#s4" target="_blank">materials and methods</a>. B. A detailed schematic of the oocyst components illustrating the absence of the outer layer of the oocyst wall (ow) following treatment with bleach. The inner layer of the wall (iw) and sporocyst walls (Spw) remain intact following bleach treatment. The mature oocyst contains two sporocysts, each with 4 sporozoites (spz).</p

Specificity between SporoAMA1 and SporoRON2-D3 is achieved through interactions within both the cysteine loop and the connecting coil.

<p>A<b>.</b> Apical view of sporoAMA1 (green surface) bound to sporoRON2-D3 (gold cartoon) (left), showing conservation of the overall AMA1/RON2 binding paradigm with generic AMA1 (purple surface) – generic RON2 synthetic peptide (sp; green cartoon) (right; PDB 2Y8T). Note that the extreme C-terminal portion of the sporoRON2 peptide is disordered as a result of its relatively “early” exit from the stabilizing environment of the hydrophobic groove and therefore is not resolved in this structure. B. Cysteine loop interactions clearly differ between sporoAMA1-sporoRON2-D3 (left) and generic AMA1-generic RON2sp (right). Hydrogen bonds shown as dotted black lines. Colored as in (A). C. Additional specificity is gained through interactions with sporoAMA1 (green surface) or generic AMA1 (purple surface) and the RON2 coil that connects the N-term helix to the cysteine loop. Central groove residue (sporoAMA1 Ser252 or generic AMA1 Tyr230) and generic AMA1 groove residue Met233 colored dark grey. Beta-hairpin loop 3 and variable loop 4 colored light grey. Side chains of sporoRON2-D3 (gold cartoon) and generic RON2sp (green cartoon) involved in specificity shown as sticks.</p