More on "HIV" gp41 25 November 2003
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Eleni Papadopulos-Eleopulos,
Biophysicist
Royal Perth Hospital, Western Australia 6001,
Valendar F Turner, John Papadimitriou, Barry Page, David Causer, Helman Alfonso

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Re: More on "HIV" gp41

More on “HIV” gp41

 

In his rapid response “Re: gp41” (24 October 2003), Christopher Noble wrote: “Eleni Papadopulos-Eleopulos claims: "Montagnier considers p41 to be the ubiquitous cellular protein actin."  He then responds:  “I have observed that Eleni often appeals to "Orthodox" authorities as supporters of her ideas. Here she tries to convince readers that Montagnier thinks that HIV-gp41 that is present in WBs and ELISAs is just cellular actin. Montagnier most certainly does not say this. To claim that he does is blatantly dishonest. A quick search of the literature demonstrates this. Montagnier coauthored a paper in 1990 which was concerned with the production of monoclonal antibodies to HIV gp41. (1)   Here it is 2003 and Eleni is still saying that Montagnier thinks HIV gp41 is actin.”

 

Montagnier most certainly did say that p45/p43/p41 is actin.  He said this in 1983 in his original paper.1   In 1984 he did not consider the p41 band diagnostic for “HIV” infection because “The 43-kD band and the 84-kDa band are cellular contaminants…”2  Neither did he consider it an “HIV” protein 1996.  In that year he omitted the gp41 band from the criteria used to define a positive “HIV” Western blot.  These criteria were: "the presence of antibodies against products of the env gene (gp160, gp120) and reactivity at least with one gag gene product”.3

 

Christopher Noble wrote: “Since 1983 the genome of HIV has been sequenced. Recombinant proteins such as gp41 have been mass produced and purified. The crystal structures have been determined by X-ray crystallography. There is a wealth of knowledge about this protein and yet Eleni still tries to claim that it is just actin.”

 

Would Christopher Noble please give us a few references which prove that the “HIV” genome and thus the nucleic acid sequences originated from “HIV” particles?

 

Would Christopher Noble please give us a few references which prove that the RNA used to mass produce recombinant proteins including gp41 originated from “HIV” particles?

 

Regardless of the wealth of knowledge including the crystal structure, would Christopher Noble please give us a few references which show that either Montagnier or anybody else has proved the existence of a protein of molecular weight of 41,000 in the “viral lysate” coded by an RNA which originated from “HIV” particles?

 

In our rapid response “gp41” (20 October 2003), we stated that “To claim that gp41 is an “HIV” protein, then (i) proof must exist that it originated from a retrovirus particles or as Montagnier put it, from purified “HIV” particles; (ii) since cellular proteins can be incorporated in virus particles, proof must exist that the protein is coded by an RNA which originated from a retrovirus particle or “purified” virus particles.”  We then asked Christopher Noble: “Would Christopher Noble please give us a few references showing that points (i) and (ii) have been satisfied?”

 

He has not responded.  If Christopher Noble continues to avoid answering this question, then it means that in his view, no such proof can be found.

 

Christopher Noble wrote: “HIV gp41 and actin have similar molecular weights. To claim that one cannot tell the difference between the two is like claiming that apples and oranges are identical because they both weigh approximately the same.”

 

Let us recapitulate a few facts:

(i)                  It is claimed that the “HIV” particles have a protein with molecular weight of 41,000 coded by the “HIV” genome which is the same molecular weight as that of actin.

(ii)                Before the AIDS era it was known that actin was incorporated in virus particles including retrovirus particles. In our extensive literature review, we have not found any studies in which the “viral lysates” are not “contaminated” with actin. In fact, in the 1997 Bess et al study, the proteins of molecular weight “near 42 kDa” (42,000) are labelled as actin with no mention whatsoever of an “HIV” protein.

(iii)               AIDS patients and those at risk have high levels of antibodies against actin. 4

 

Let us assume that Christopher Noble repeats Gallo’s and Montagnier’s experiments.   That is, he takes the “viral lysate” and reacts it with AIDS patient sera.    What will be the scientific basis for a conclusion that the protein of molecular weight of 41,000 which reacts with AIDS patient’s sera is not actin but a protein coded by the genome of a totally new virus?

 

Christopher Noble wrote: “The fact that these recombinant proteins react with sera from AIDS patients is not just an accidental coincidence as Eleni would have you believe. It is evidence that demands explanation. Eleni has no explanation for this experimental evidence. Her theory cannot predict this. She would like you to believe that this reaction is just non-specific. This is not true HIV-1 group O gp41 recombinant antigens are specific to sera from patients who also have detectable HIV-1 group O RNA in their blood.”

 

It is a known fact that the sera from AIDS patients and those at risk react with a plethora of non-“HIV” proteins and other antigens.  In 1993 Montagnier wrote: “These results illustrate the influence of carbohydrates moieties on the specificity of the antibodies produced and clearly indicate that such procedures may be an efficient way to raise specific immune responses that are not type specific.   Moreover, this cross-reactivity might explain the double-positive reactivity observed, in some human sera, against both HIV-1 and HIV-2 envelope antigens.5

 

According to Gallo, the antibodies which react with glycoproteins are not directed against the polypeptide portions of the proteins “but against the carbohydrate moieties on the molecule that are introduced by the host cell as a post-transcriptional event, and which are therefore cell-specific and not virus-specific”.6  It is highly significant how Gallo reached this conclusion. 

 

In the mid 1970s Gallo and his colleagues reported the isolation of the “first” human retrovirus, HL23V. In fact, the evidence for the "isolation" of HL23V surpassed that of “HIV” in at least two aspects. Unlike “HIV” Gallo's group: (i) reported the detection of reverse transcriptase activity in fresh, uncultured leucocytes;7 (ii) published an electron micrograph of virus‑like particles banding at a sucrose density of 1.16 gm/ml.8 Following the discovery of HL23V, some researchers attempted to determine its prevalence utilising antibody tests9 while others were interested to determine the specificity of the antibody reactions. The former included two of the best known HIV experts, Reinhard Kurth and Robin Weiss, and their colleagues who, for this purpose used "the simian sarcoma-associated helper virus (SSAV) and the M7 strain of baboon endogenous virus (BEV) to survey human sera for specific antibodies. Also included is a virus (HL23V-1) originally isolated from cultured peripheral blood leukocytes of a patient with acute myelogenous leukemia…A survey of human sera from healthy individuals revealed the presence of naturally occurring antibodies that react in radioimmunoprecipitation assays with proteins of mammalian type-C viruses" including the internal (gag) and envelope (env) proteins of HL23V, SSAV and BEV and concluded, "The serological studies presented here and by others provide indirect evidence that the infectious mode of transmission remains a real possibility in humans, and suggests that infection with an oncornavirus [retrovirus] may be extremely widespread".10 Three years later, in 1980, two research groups,11 12 one from the Laboratory of Cellular and Molecular Biology, National Cancer Institute and the other from the Laboratory of Viral Oncology, Memorial Sloan‑Kettering Cancer Center, using the "viral glycoproteins", found that the antibodies present in human sera which reacted with these proteins were "directed against carbohydrate structures" and concluded that "The results are consistent with the idea that the antibodies in question are elicited as a result of exposure to many natural substances possessing widely cross‑reacting antigens and are not a result of widespread infection of man with replication competent oncoviruses".  In 1981 Gallo accepted the evidence that the antibodies which reacted with proteins of HL23V were directed not against the proteins "but against the carbohydrate moieties on the molecule that are introduced by the host cell as a post‑transcriptional event, and which are therefore cell‑specific and not virus‑specific".6 This discovery was of such significance that today nobody, not even Gallo, considers HL23V as being the first human retrovirus, or even a retrovirus. In fact, in 1981 when Gallo and his colleagues reported the presence in humans of antibodies to what he now calls the first human retrovirus, HTLV-I, (according to Weiss, "The first 'human' retrovirus to be isolated in 1971 was human foamy virus (HFV) from a nasopharyngeal carcinoma line",13) the title of the paper was, "Antibodies in human sera reactive against an internal structural protein of human T-cell lymphoma virus".6  At present there is ample evidence to show that antibodies directed against carbohydrate react with the “HIV” glycoproteins.14 15

 

References

 

1. Barré-Sinoussi F, Chermann JC, Rey F, Nugeyre MT, Chamaret S, Gruest J, et al. Isolation of a T-lymphotropic retrovirus from a patient at risk for acquired immune deficiency syndrome (AIDS). Science 1983;220:868-71.

2. Brun-Vezinet F, Rouzioux C, Montagnier L, Chamaret S, Gruest J, Barre-Sinoussi F, et al. Prevalence of antibodies to lymphadenopathy-associated retrovirus in African patients with AIDS. Science 1984;226:453-456.

3. Chamaret S, Squinazi F, Courtois Y, Montagnier L. Presence of anti-HIV antibodies in used syringes left out in public places, beaches or collected through exchange programs. Mo. D. 1947. In Procedings XIth International Conference on AIDS, 1996 Vancouver.

4. Matsiota P, Chamaret S, Montagnier L. Detection of Natural Autoantibodies in the serum of Anti-HIV Positive-Individuals. Ann Inst Pasteur Immunol 1987;138:223-233.

5. Benjouad A, Gluckman JC, Montagnier L, Bahraoui E. Specificity of antibodies produced against native or desialylated human immunodeficiency virus type 1 recombinant gp160. J Virol 1993;67:1693-7.

6. Kalyanaraman VS, Sarngadharan MG, Bunn PA, Minna JD, Gallo RC. Antibodies in human sera reactive against an internal structural protein of human T-cell lymphoma virus. Nature 1981;294:271-273.

7. Gallo RC, Wong-Staal F, Reitz M, Gallagher RE, Miller N, Gillespie DH. Some evidence for infectious type-C virus in humans. In: Balimore D, Huang AS, Fox CF, editors. Animal Virology. New York: Academic Press Inc., 1976:385-405.

8. Gallagher RE, Gallo RC. Type C RNA Tumor Virus Isolated from Cultured Human Acute Myelogenous Leukemia Cells. Science 1975;187:350-353.

9. Teich NM, Weiss RA, Salahuddin SZ, Gallagher RE, Gillepsie DH, Gallo RC. Infective transmission and characterisation of a C-type virus released by cultured human myeloid leukaemia cells. Nature 1975;256:551-555.

10. Kurth R, Teich NM, Weiss R, Oliver RTD. Natural human antibodies reactive with primate type-C antigens. Proceedings of the National Academy of Sciences of the United States of America 1977;74:1237-1241.

11. Barbacid M, Bolognesi D, Aaronson SA. Humans have antibodies capable of recognizing oncoviral glycoproteins: Demonstration that these antibodies are formed in response to cellular modification of glycoproteins rather than as consequence of exposure to virus. Proceedings of the National Academy of Sciences of the United States of America 1980;77:1617-1621.

12. Snyder HW, Fleissner E. Specificity of human antibodies to oncovirus glycoproteins: Recognition of antigen by natural antibodies directed against carbohydrate structures. Proceedings of the National Academy of Sciences of the United States of America 1980;77:1622-1626.

13. Weiss RA. Retrovirus classification and cell interactions. J Antimicrob Chemother 1996;37:B. 1-11.

14. Papadopulos-Eleopulos E, Turner VF, Papadimitriou JM, Causer D. HIV antibodies: Further questions and a plea for clarification. Curr Med Res Opinion 1997;13:627-634.

15. Papadopulos-Eleopulos E, Turner VF, Papadimitriou JM, Causer D, Page B. HIV antibody tests and viral load - more unanswered questions and a further plea for clarification. Curr Med Res Opinion 1998;14:185-186.

 

 

Competing interests: None declared