ACT FOUR-Blood Jaguars
HORSETAIL
FAMILY: Equisetaceae
GENUS: EqUlSetum
SPECIES: Arvense
COMMON NAME: Field Horsetail
ETHNIC NAMES: At Quyroughi, Atkuyrugu, Chieh Hsu
Ts'Ao, Cola de Caballo, Equiseto Menor, Kilkah Asb,
Prele, Sugina, Thanab al Khail, Vara de Oro, Wen Ching
PROPERTIES/ACTIONS: Astringent, Antiinflammatory,
Diuretic, Antihemorrhagic
CHAPTER TWELVE
Lake Crossing
AUGUST 15, B:i i A.M.
INSTAR INSTITUTE
LANGLEY VIRGINIA
Lauren slid the magnetic security card through the lock on her office door and entered. It was the first chance she'd had to return to her office in the past day. Between stretches in the institute's hospital ward visiting Jessie and meetings with various MEDEA members, she hadn't had a moment to herself. The only reason she had this free moment was that Jessie seemed to be doing very well. Her temperature continued to remain normal, and her attitude was growing brighter with every passing hour.
Cautiously optimistic, Lauren began to hope that her initial diagnosis had been mistaken. Maybe Jessie did not have the jungle disease. Lauren was now glad she had kept silent about her fears. She could have needlessly panicked Marshall and Kelly. Lauren may have indeed placed too much confidence in Alvisio's statistical model. But she could not fault the epidemiologist. Dr. Alvisio had indeed warned her his results were far from conclusive. Further data would need to be collected and correlated.
But then again, that pretty much defined all the current levels of investigation. Each day, as the disease spread through Florida and the southern states, thousands of theories were bandied about: etiological agents, therapeutic protocols, diagnostic parameters, quarantine guidelines. Instar had become the nation's think tank on this contagion. It was their job to ferret through the maze of scientific conjecture and fanciful epidemiological models to glean the pearls from the rubbish. It was a daunting task as data flowed in from all corners of the country. But they had the best minds here.
Lauren collapsed into her seat and flicked on her computer. The chime for incoming mail sounded. She groaned as she slipped on a pair of reading glasses and leaned closer to the screen. Three hundred and fourteen messages waited. And this was just her private mailbox. She scrolled down the list of addresses and skimmed the subject lines, searching through the little snippets for anything important or interesting.
Inbox
From Subject
jptdvm@davls.ut.arg re: simian blosimilarities
treat magnus@scriabs.com call for sample standardization
5y5telnattCa@fdC.gaV prog. report
xreynalds@largebio.cam large stale biological labs
synergyrneds@phdrugs.torn pharmacv question
gerard@dadecounty.tfil.gov quarantine projection
brt@washingtonpost.org request for Interview
As she scrolled down, one name caught her eye. It was oddly familiar, but she could not remember exactly why. She brought her computer's pointer to the name: Large Scale Biological Labs. She crinkled her nose in thought, then it came to her. The night Jessie's fever developed, she had been paged by this same outfit. Well after midnight, she recalled. But the sick child had distracted her from following up on the page.
It probably wasn't important, but she opened the e-mail anyway, her curiosity now aroused. The letter appeared on the screen. Dr. Xavier Reynolds. She smiled, instantly recognizing the name. He had been a grad student of hers years ago and had taken a position at some lab in California, perhaps this same lab. The young man had been one of her best students. Lauren had attempted to recruit him into the MEDEA group here at Instar, but he had declined. His fiance had accepted an associate professorship at Berkeley, and he had naturally not wanted to be separated.
She read his note. As she did, the smile on her lips slowly faded.
From: xreynolds@largebio.com
Date: 14 Aug 13:48:28
To: lauren obrienQinstar.org
Subject: Large Scale Biological Labs
Dr. O'Brien:
Please excuse this intrusion. I attempted to page you last night, but I assume you're very busy. So I'll keep this brief.
As with many labs around the country, our own is involved in researching the virulent disease, and I think I've come across an intriguing angle, if not a possible answer to the root puzzle: What is causing the disease? But before voicing my findings, I wanted to get your input.
As head of the proteonomic team here at Large Scale Biological Labs, I have been attempting to index mankind's protein genome, similar to the Human Genome Project for DNA. As such, my take on the disease was to investigate it backward. Most disease-causing agents-bacteria, viruses, fungi, parasites-do not cause illness by themselves. It is the proteins they produce that trigger clinical disease. So I hunted for a unique protein that might be common to all patients.
And I found one! But from its folded and twisted pattern, a new thought arose. This new protein bears a striking similarity to the protein that causes bovine spongiform encephalopathy. Which in turn raises the question: Have we been chasing the wrong tail in pursuing a viral cause for this disease?
Has anyone considered a prion as the cause?
For your consideration, I've modeled the protein below.
Title: unknown prion (?)
Compound: folded protein w/ double terminal alpha helixes
Model:
Exp. Method: X-ray diffraction
EC Number: 3.4.1.18
Source: Patient #24-b12, Anawak Tribe, lower Amazon
Resolution: 2.00 R-Value: 0.145
Space Group: P21 20 21
Unit cell:
dim: a 60.34 b 52.02 c 44.68
angles: alpha 90.00 beta 90.00 gamma 90.00
Polymer chains: 156L Residues: 144
Atoms: 1286
So there you have the twisted puzzle. As I value your expertise, Dr. O'Brien, I would appreciate your thoughts, opinions, or judgments before promoting this radical theory.
Sincerely, Xavier Reynolds, Ph.D.
"A prion:" Lauren touched the diagram of the molecule. Could this indeed be the cause?
She pondered the possibility. The word prion was scientific shorthand for "proteinaceous infectious particle:" The role of prions in disease had only been documented within the last decade, earning a U.S. biochemist the 1997 Nobel Prize. Prion proteins were found in all creatures, from humans down to single-celled yeast. Though usually innocuous, they had an insidious duality to their molecular structure, a Jekyll-and-Hyde sort of thing. In one form, they were safe and friendly to a cell. But the same protein could fold and twist upon itself, creating a monster that wreaked havoc on cellular processes. And the effect was cumulative. Once a twisted prion was introduced into a host, it would begin converting the body's other proteins to match, which in turn converted its neighbors, spreading exponentially through the host's systems. Worse, this host could also pass the process to another body, a true infectious phenomenon.
Prion diseases had been documented both in animals and man: from scabies in sheep to Creutsfeldt-Jacob disease in humans. The most well-known prion disease to date was one that crossed between species. Dr. Reynolds had mentioned it in his letter: bovine spongiform encephalopathy, or more commonly, mad cow disease.