posted
I did read that & all of the links to the other 3 threads. I just don't understand all of the lingo.
Isn't band 41 indicative of many things, not just Bb?
My doctor (Dr. S in SE PA) agreed that it was negative (from IGeneX) but IGeneX includes that note about one double starred band being positive possibly indicating clinical significance - why don't they just say the test result is positive?
I wonder what any other LLMD would say.
~Erin
-------------------- ~Erin Posts: 58 | From SE PA | Registered: May 2006
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geniveve
Unregistered
posted
ok, i'm with you. igenex showed only two bands for 39 and 41 and said i was positive. only one little bity star i'm positive. my doc tested for everything under the sun, so no coinfections, nothing. igm negative. elisa and western block negative.
i have friends who have multiple stars, 3 and 4 in practically every band, and i only have two.
guess i don't understand but my symptoms do say lyme.....i have almost all of the symptoms and did have the em.
cantgiveupyet
Frequent Contributor (1K+ posts)
Member # 8165
posted
Bottom line is there is no reliable test for lyme and that is why it has to be a clinical diagnosis.
my IGM was pos for 41 IND for 31 IGM pos 41,66 IND 39. CDC doesnt allow band 31 because of the vaccine. go figure i never had it.
Im so sick the only thing i test pos for is yeast via culture......why, because there is a reliable test for it.
-------------------- "Say it straight simple and with a smile."
"Thus the task is, not so much to see what no one has seen yet, But to think what nobody has thought yet, About what everybody sees."
-Schopenhauer
pos babs, bart, igenex WB igm/igg Posts: 3156 | From Lyme limbo | Registered: Oct 2005
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janet thomas
Frequent Contributor (1K+ posts)
Member # 7122
posted
Band 41 can be any spirochete and so means little, 39 is specific for Lyme and by itself is sufficient.
-------------------- I am not a doctor and this is not medical advice but only my personal experience and opinion. Posts: 2001 | From NJ | Registered: Mar 2005
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"Western blots look for antibodies. These antibodies are made by your immune system. In this case, the antibodies are made to fight against different parts of the Lyme bacteria, which is called Borrelia burgdorferi, and other Borrelia species. In other words, your immune system does not make one big antibody against the whole bacteria. So, when you see a number on a borreliosis Western blot, it corresponds to a specific part of the bacteria.
Compare it to the old story of different blind people touching an elephant. Based on the part of the elephant each one touched, each person had their own perception. Likewise, the antibodies attach to different and specific parts of Borrelia burgdorferi.
Numbers on Western blots correspond to weights. Kilodaltons (kDa) are the units used for these microscopic weights. Think of it like pounds or ounces. An 18 kDa antibody weighs 18 kilodaltons. To do a Western blot, thin gel strips are impregnated with the various parts of Borrelia burgdorferi. Each of the numbers, 18 through 93, on the test result form, is a part of the bacteria.
Blood is made up of red blood cells and serum; Spinning blood in a centrifuge separates serum from red blood cells and other things, like white blood cells and platelets.
Serum contains antibodies made by the immune system. Electricity is used to push the serum through the thin gel strips for the Western blot. If there are any antibodies against parts of Borrelia burgdorferi present in your serum, and these parts are impregnated on the strip, the antibody will complex (bind) to that part."
-------------------- --Lymetutu-- Opinions, not medical advice! Posts: 96222 | From Texas | Registered: Feb 2001
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posted
I thouhgt I remembered a recent post where someone posted what else could causespecific bands to be +.
Bands 58 & 66 are heat something - I don't understand that.
Is Syphillis the only other bacteria that can cause positives?
~Erin
-------------------- ~Erin Posts: 58 | From SE PA | Registered: May 2006
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treepatrol
Honored Contributor (10K+ posts)
Member # 4117
posted
quote:Originally posted by metasequoia: I thouhgt I remembered a recent post where someone posted what else could causespecific bands to be +.
Bands 58 & 66 are heat something - I don't understand that.
Is Syphillis the only other bacteria that can cause positives?
~Erin
IgG WESTERN BLOT
The IgG Western Blot is a sandwich-type immunoassay performed in a manner that allows visualization of the patient's antibodies. It is a qualitative test and is generally more sensitive and specific than the ELISA. This test must be used if the Lyme IgG/IgM antibody serology is equivocal or positive. The somewhat-specific Lyme antibodies of importance are against the following molecular weights of the B. burgdorferi antigens: 23-25 kDa (Osp C); 31 kDa (Osp A); 34 kDa (Osp B); 39 kDa; 41 kDa; and 83-93 kDa7. "kDa" is the abbreviation for "kilodalton," which is used for molecular weight designations. "Osp" refers to outer surface protein of the bacteria.
There are currently multiple criteria that support a positive blot. "Positive" means that certain antibodies to B. burgdorferi are present. The CDC/ASTPHLD criteria are very conservative, require 5 of 10 bands (antibodies) for a positive result, and do not recognize equivocal or borderline results.8,9 These criteria would be more appropriate for a formal clinical study during early Lyme disease.
IGeneX has several years of clinical data that support more liberal reporting criteria.10 In addition, current studies show that the CDC/ASTPHLD criteria miss some patients with culture-proven erythema migrans (EM).5,11 Both the IGeneX and the CDC/ASTPHLD criteria are included on the IGeneX report form sent to the physician. 3,5,8,9
The Western Blot involves a highly complex visual determination of protein bands, based on their molecular weights and intensities. The IGeneX report form provides an interpretation along with the results in detail.
A positive IgG result with clinical history may be indicative of Lyme disease. Patients with other spirochetal disease and/or who test positive for rheumatoid factor or Epstein Barr virus may have cross-reacting antibodies. A positive response in this, as in any antibody assay, indicates sensitization, not necessarily active disease. 12
Figure 4. Significant antibodies detected by Western Blot (Lane 1 has kDa marker proteins)
IgM WESTERN BLOT
The IgM Western Blot is a very sensitive indicator of exposure to B. burgdorferi. It may be positive as early as one week after a tick bite, and will usually remain positive for six to eight weeks after the initial exposure. Re-exposure and recurrent disease also cause this test to be positive for a period of time. For the testing to be complete, the IgM blot should be run along with the IgG blot. However, for economic reasons, the IgG blot may be run first: when the IgG blot is negative, the IgM blot should be performed.
The antibody specificities of importance for the IgM blot are similar to those for the IgG blot (with the exception of 83-93 kDa, which is still being investigated for significance). The CDC/ASTPHLD criteria for a positive result are two of the following three bands: 23-25 kDa (Osp C); 39 kDa; and/or 41 kDa.8,9 IGeneX adds the 31 kDa (Osp A), and/or the 34 kDa (Osp B) to the criteria,10,12 with the argument that these two antigens are used for the vaccines and therefore their antibodies should be included in the interpretation of positivity. The IgM Western blot is often positive in patients with persistent infection.6 Sometimes it is the only antibody marker detected.
When the IgM ELISA is equivocal or positive, the IgM Western blot must be performed. In addition, because the literature suggests that rheumatoid conditions may lead to false positive IgM antibody responses, an ANA/DNA/rheumatoid factor screen may be ordered to rule out false positive reactions. Patients testing positive with serologic tests for syphilis may also test positive for the Lyme antibody tests.13-15
A positive IgM result with clinical history may be indicative of early Lyme disease or persistent infection in otherwise serologically negative individuals. Recently reported data support our observation that some Lyme patients may have only a restricted IgM response to B. burgdorferi. 16,17
Similar to the IgG Western blot, the IgM Western blot involves a highly complex visual determination of protein bands, based on their molecular weights and intensities. For both tests, IGeneX uses multiple negative controls to serve as baselines for comparison to positive responses.
The IGeneX report form provides an interpretation along with the results in detail.
IgM to antigens of 39, 58, 60, 66, or 93 kDa, conversely, were most often seen in sera obtained within 1 month postbaseline. Their presence may be of assistance in confirming a recent infection with B. burgdorferi in individuals living in areas where Lyme disease is endemic.
Heat shock proteins {HSP} are a group of proteins whose expression is increased when the cells are exposed to elevated temperatures. This increase in expression is transcriptionally regulated. This dramatic upregulation of the heat shock proteins induced mostly by Heat Shock Factor {HSF} is a key part of the heat shock response.
Production of high levels of heat shock proteins can also be triggered by exposure to different kinds of environmental stress conditions, such as infection, inflammation, exposure of the cell to toxins {ethanol, arsenic, trace metals and ultraviolet light, among many others}, starvation, hypoxia {oxygen deprivation}, nitrogen deficiency {in plants}, or water deprivation.
Consequently, the heat shock proteins are also referred to as stress proteins and their upregulation is sometimes described more generally as part of the stress response.
Scientists have not discovered exactly how heat-shock {or other environmental stressors} activates the heat-shock factor. However, some studies suggest that an increase in damaged or abnormal proteins brings HSPs into action.
Heat-shock proteins are present in all cells at all biological levels. They appear when the cell is under heat stress {or other stress}.
Heat-shock proteins also occur under non-stressful conditions, simply "monitoring" the cell's proteins. Some examples of their role as "monitors" are that they carry old proteins to the cell's "recycling bin" and they help newly synthesised proteins fold properly. These activities are part of a cell's own repair system, called the "cellular stress response" or the "heat-shock response."
The function of heat-shock proteins is similar in virtually all living organisms, from bacteria to humans.
Heat shock proteins are molecular chaperones for protein molecules. They are usually cytoplasmic proteins and they perform functions in various intra-cellular processes.
They play an important role in protein-protein interactions such as folding and assisting in the establishment of proper protein conformation {shape} and prevention of unwanted protein aggregation. By helping to stabilize partially unfolded proteins, HSPs aid in transporting proteins across membranes within the cell. Some members of the HSP family are expressed at low to moderate levels in all organisms because of their essential role in protein maintenance.
The HSPs are named according to their molecular weights, for example Hsp70 and Hsp90 each define families of chaperones. The major classes of heat shock proteins are tabulated below.
Potential applications Heat-shock proteins are of potential interest to cancer researchers, based on research that has shown that animals may respond to cancer "vaccinations." Tumor cells were "attenuated" (or weakened) and injected in small quantities into a rodent, causing the rodent to become immune to future full-fledged tumor-cell injections. While any relevance of animal research to humans has not been established, it is possible that the same may hold true for other species.
Some researchers are conducting research on using heat shock proteins in the treatment of cancer. Some researchers speculate that HSPs may be involved in binding protein fragments from dead malignant cells and presenting them to the immune system.
Researchers are also investigating the role of HSPs in conferring stress tolerance to hybridized plants, hoping to address drought and poor soil conditions for farming.
Researchers Many years after the tumor cell attenuation research was done, Pramod Srivastava discovered that the specific part of the cell that was protecting the "immune" mice was the heat-shock proteins.
Susan Lindquist is currently a leading heat-shock protein researcher. She is investigating, among other things, "how HSPs are regulated, and how they function to protect organisms from death and from developmental anomalies induced by heat." - from her faculty page at:
Chaperones and heat shock proteins The principal heat-shock proteins that have chaperone activity belong to five conserved classes: HSP100, HSP90, HSP70, HSP60 and the small heat-shock proteins (sHSPs).
Approximate molecular weight (kDa) Prokaryotic proteins Eukaryotic proteins Function
10 kDa GroES Hsp10 20-30 kDa GrpE The HspB group of Hsp. Ten members in mammals including Hsp27 or HspB1 40 kDa DnaJ Hsp40 60 kDa GroEL, 60kDa antigen Hsp60 70 kDa DnaK The HspA group of Hsp including Hsp71, Hsc70, Hsp72, Grp78, BiP, Hsx70 found only in primates Protein folding and unfolding, provides thermotolerance to cell on exposure to heat stress
90 kDa HtpG, C62.5 The HspC group of Hsp including Hsp90, Grp94 Maintenance of steroid receptors and transcription factors 100 kDa ClpB, ClpA, ClpX Hsp104, Hsp110 Tolerance of extreme temperature
Although the most important members of each family are tabulated here, it should be noted that some species may express additional chaperones, co-chaperones, and heat shock proteins not listed. Additionally, many of these proteins may have multiple splice variants {Hsp90α and Hsp90β, for instance} or conflicts of nomenclature (Hsp72 is sometimes called Hsp70).
-------------------- Do unto others as you would have them do unto you. Remember Iam not a Doctor Just someone struggling like you with Tick Borne Diseases.
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