Bob,
I am seeing where your worms are dependent on the host for the polyamines that have interested me for so long. So, if the host is producing too much polyamines (as I hypothesize) then the worms would be of value in absorbing the excess and dampening the problems of increased polyamines. And EBV, that Bromley points to, does induce the host B cell's MYC, which increases ornithine decarboxylase activity, which is the initial step in polyamine synthesis. Interesting parallels, perhaps even fitting together.
Wesley
http://www.ncbi.nlm.nih.gov/pubmed/1993461
Polyamine metabolism in some helminth parasites.Sharma V, Tekwani BL, Saxena JK, Gupta S, Katiyar JC, Chatterjee RK, Ghatak S, Shukla OP.
Division of Biochemistry, Central Drug Research Institute, Lucknow, India.
Polyamine levels of some helminth parasites were analyzed by reverse phase HPLC of benzoyl derivatives. Setaria cervi, Acanthocheilonema viteae, Hymenolepis nana, H. diminuta, and Ascaridia galli contained higher levels of spermine than spermidine while in Ancylostoma ceylanicum and Nippostrongylus brasiliensis the spermidine levels were higher than spermine; putrescine was either absent or present in minor quantities. The enzymes of polyamine biosynthesis viz., ornithine decarboxylase, S-adenosyl methionine (SAM)-decarboxylase, and arginine decarboxylase were present in very low to negligible amounts in all the parasites examined. A. ceylanicum exhibited high activity of ornithine amino transferase (OAT) and catalyzed appreciable decarboxylation of ornithine. The ornithine decarboxylating activity of A. ceylanicum was localized in the particulate fraction containing mitochondria, not inhibited by alpha-difluoromethyl ornithine, the specific inhibitor of ornithine decarboxylase (ODC), but inhibited in the presence of glutamate, suggesting the involvement of mitochondrial OAT rather than a true ODC in ornithine decarboxylation in this parasite. Significant activity of polyamine oxidase was also detected in helminth parasites. The absence of polyamine biosynthesizing enzymes in helminth parasites suggests their dependence on hosts for uptake and interconversion of polyamines, providing a potential target for chemotherapy.