Classifications

• • C—CHEMISTRY; METALLURGY
  • C07—ORGANIC CHEMISTRY
  • C07K—PEPTIDES
  • C07K16/00—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies
  • C07K16/18—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies against material from animals or humans
  • C07K16/28—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants
  • C07K16/2803—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against the immunoglobulin superfamily
• • A—HUMAN NECESSITIES
  • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
  • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
  • A61P29/00—Non-central analgesic, antipyretic or antiinflammatory agents, e.g. antirheumatic agents; Non-steroidal antiinflammatory drugs [NSAID]
• • A—HUMAN NECESSITIES
  • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
  • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
  • A61P31/00—Antiinfectives, i.e. antibiotics, antiseptics, chemotherapeutics
  • A61P31/12—Antivirals
  • A61P31/14—Antivirals for RNA viruses
  • A61P31/18—Antivirals for RNA viruses for HIV
• • A—HUMAN NECESSITIES
  • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
  • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
  • A61P35/00—Antineoplastic agents
• • A—HUMAN NECESSITIES
  • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
  • A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
  • A61P37/00—Drugs for immunological or allergic disorders
• • C—CHEMISTRY; METALLURGY
  • C07—ORGANIC CHEMISTRY
  • C07K—PEPTIDES
  • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
  • C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
  • C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
  • C07K14/70503—Immunoglobulin superfamily
• • A—HUMAN NECESSITIES
  • A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
  • A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
  • A61K38/00—Medicinal preparations containing peptides

Definitions

• AAMP-l A PROTEIN WITH LOCAL HOMOLOGIES TO HIV-1 ENV AND NEF PROTEINS.
• the present invention relates, in general, to AAMP-l.
• the present invention relates to a DNA segment encoding AAMP- 1; polypeptides encoded by the DNA segment; recombinant DNA molecules containing the DNA segment; cells containing the recombinant DNA molecule; a method of producing AAMP-l; antibodies specific to AAMP-l; and a method of measuring the amount of AAMP-l in a sample.
• the major histocompatibility complex class II proteins have recently been found to contain local homologies to the HIV-1 envelope protein (H. Golding et al., J. EXP. Med. 167, 914 (1988); H. Golding et al., J. Clin. Invest. 83, 1430 (1989); J. A. T. Young, Nature 332, 215 (1988)). Such homologous regions may serve as targets for antibodies generated to HIV-l proteins and thus compromise the immune system in AIDS. Golding et al. (J. EXP. Med.
• HIV-l gp41-envelope protein has identified a common epitope located in the carboxy terminus of the HIV-l gp41-envelope protein and the amino terminal portion of the beta chain of all human HLA class II antigens. Although the epitope is small, 5 consecutive identities or similarities, they found that it is an effective example of "molecular mimicry n in that monoclonal antibodies raised against synthetic peptides from each protein react interchangeably with native HIV-l envelope and MHC class II molecules.
• One third of HIV-l positive individuals were shown to have serum antibodies directed against peptides derived from HIV-l envelope protein, the homologous peptide from the MHC class XI molecules, and native MHC class II molecules (H. Golding et al. J. EXP. Med. 167, 914 (1988)).
• Two other regions of the HLA class II beta chain and another immune related protein, interleukin-2 also show limited homology to HIV-l (J. A. T.
• HIV-l vaccine development An important consideration in HIV-l vaccine development is the potential existence of additional host cell surface proteins with ho ologies to HIV-l that may crossreact with antibodies directed against its peptides.
• the present invention relates to the protein AAMP-l which has immunoglobulin (Ig) type domains that contain strong local homologies to conserved regions of the HIV-l envelope and nef proteins.
• Ig immunoglobulin
• FIG. 1 Nucleotide sequence of human A2058 melanoma cell AAMP-l cDNA isolated from a lambda gtll expression library with its predicted amino acid sequence.
• the phage insert, AAMP-l was subcloned into Bluescript plasmid (Stratagene) for production of double stranded cDNA for sequencing using the dideoxynucleotide termination method (F. Sanger et al. Proc. Natl. Acad. Sci. USA 74, 5463 (1977)) with Sequenase 2.0 (U.S. Biochemical) .
• Nucleotide residues are numbered beginning at the 5' end. Amino acid sequence numbering begins with the first methionine
• FIG. 1 Northern blot of human melanoma A2058 cells probed with AAMP-l cDNA. A single 1.6Kb band is seen on blots of total cytoplas ic (Lane 1) and polyadenylate-enriched (Lane 2) A2058 RNA.
• Total cytoplasmic RNA, 41 micrograms ( ⁇ g) was isolated from 6 million cells lysed in Nonidet P-40 (0.65%), separated into an aqueous phase in the presence of 7M urea, 1% sodium dodecyl sulfate, Tris buffer, NaCl, and EDTA, followed by phenol/chloroform extraction.
• RNA 2.2 ⁇ g, enriched for messenger RNA
• RNA was isolated from 16 million cells with a Fast Track Kit Version 2.1 (Invitrogen Corp. San Diego, CA) .
• RNA was denatured in formaldehyde, electrophoresed in a 1% agarose/formaldehyde gel, transferred to Schlelcher & Schnell Nytran nylon membrane and crosslinked with ultraviolet light.
• the 1766 bp AAMP-l cDNA was labeled with (alpha-"P) dCTP (NEN Research Products, Boston, MA) using random priming. Hybridization overnight at 65*C was performed according to Church and Gilbert (Proc. Natl. Acad. Sci 81, 1991 (1984)).
• FIG. 3 Northern blot of AAMP-l expression in human T-cell activation. Hours refer to time in culture.
• A AAMP-l single 1.6Kb message.
• B Beta-2 micro-globulin standard.
• Lanes 1-3 Non-stimulated human CD4+ T cells (Human peripheral blood mononuclear cells from normal donors were separated by Ficoll-Hypaque density-gradient centrifugation. Unstimulated CD4+lymphocytes were obtained by rigorous immunomagnetic negative selection with Advanced Magnetic Particles (Advanced Magnetic, Cambridge, MA) or Dynabeads (Dynal Inc., Fort Lee, NJ) both bound to goat anti-mouse lgG. Negative selection was performed as described (K. J. Horgan and S.
• mAbs consisting of anti-HLA class II mAb (IVA12) , CD20 mAb (1F5) , CD16 mAb (3G8) , CDllb mAb (NIHllb-1), CD14 mAb (MMA) , CD8 mAb (B9.8), and mAb against glycophorin (10F7) . Purity of the isolated cells was greater than 98%.
• the selected CD4+ T-cell ⁇ were free of monocytes based on the lack of proliferative response to optimal concentrations (1/200 dilution) of Phytohe agglutinin (M form) (PHA) (GIBCO, Grand Island, NY)), lanes 1 and 2 at 0 and 24 hours, respectively, without mitogen stimulation, and lane 3 after 12 hours in the presence of the protein synthesis inhibitor, cycloheximide, which has been frequently observed to stabilize certain mRNA species (K. Kelly et al. P. Leder, Cell 35, 603 (1983)). Lanes 4-8: CD4+T cells activated ". (T-cell activation assays were performed using > ⁇ standard techniques.
• T-cell ⁇ 10 million purified CD4+ T-cell ⁇ were cultured in 35 mm flat bottom wells for various time periods in culture medium (RPM1 1640 (Hazelton Biologies Inc. Lenexa, KS) supplemented with 20 mM glutamine (Hazelton) , 10% heat inactivated fetal calf serum (Biofluids, Rockville, MD) , 100 IU/ml of penicillin, and 100 ⁇ g/ l streptomycin) , either unstimulated or stimulated with antibodies bound to the wells.
• T- cell stimulatory conditions were as described (G. A. van Seventer et al. Eur. J. jp ..nr>7 - 21, 1711 (1991)).
• Monoclonal antibodies were immobilized on the plastic of the well by dilution in phosphate buffered saline (PBS) and overnight incubation at 4*C, followed by washing with PBS.
• the CD3 mAb, OKT3, and the CD2 mAb, 95-5-49, were applied at 1 ⁇ g and 10 ⁇ g, purified j/ml --- respectively, all in a volume of 3 milliliters per well.
• Monoclonal antibodies were used as purified immunoglobulin derived from ascites fluid; CD2 mAb (directed against the Tll.l epitope): 95-5-49, lgGl (hybridoma kindly provided by Dr. R. R.
• RNA samples were prepared from CD4+ T cells by the guanidinium isothiocyanate-cesiu chloride method of Maniatis et al. (T. E. Maniatis, E. F. Fritsch, J. Sambrook, Molecular Clonin g : A aboratory MfllWal (Cold Spring Harbor Laboratory, Cold Spring Harbor, New York, ed. 2, 1989), pp.
• the present invention relates to a DNA segment coding for a polypeptide comprising an amino acid sequence corresponding to AAMP-l, or at least 5 contiguous amino acids thereof.
• the DNA segment comprises the sequence shown in SEQ ID NO: 1
• the DNA segment encodes the amino acid sequence set forth in SEQ ID NO:2, allelic or species variation thereof, or at least 5 contiguous amino acids thereof (preferably, at least 5, 10, 15, 20, 30 or 50 contiguous amino acids thereof) .
• the present invention relates to a polypeptide free of proteins with which it is naturally associated or a polypeptide bound to a solid support and comprising an amino acid sequence corresponding to AAMP-l, or at least 5 contiguous amino acids thereof (preferably, at least 5, 10, 15, 20, 30 or 50 contiguous amino acids thereof) .
• the polypeptide comprises the amino acid sequence set forth in SEQ ID NO:2, or allelic or species variation thereof equivalent thereto (for example, immunologically or functionally, equivalent thereto) , or at least 5 contiguous amino acids thereof (preferably, at least 5, 10, 15, 20, 30 or 50 contiguous amino acids thereof) .
• the present invention relates to a recombinant DNA molecule comprising a vector (for example plasmid or viral vector) and a DNA segment (as described above) coding for a polypeptide corresponding to AAMP-l; as described above.
• the encoding segment is present in the vector operably linked to a promoter.
• the present invention relates to a cell containing the above described recombinant DNA molecule. Suitable host cells include procaryotes (such as bacteria, including E_j. coli) and both lower eucaryotes (for example yeast) and higher eucaryotes (for example, mammalian cells) . Introduction of the recombinant molecule into the cell can be effected using methods known in the art.
• the present invention relates to a method of producing a polypeptide having an amino acid sequence corresponding to AAMP-l comprising culturing the above-described cell under conditions such that the DNA segment is expressed and the polypeptide thereby produced and isolating the polypeptide.
• the present invention relates to an antibody having binding affinity for AAMP-l, or a unique portion thereof.
• AAMP-l comprises the amino acid sequence set forth in SEQ ID NO:2, allelic or species variation thereof, or at least 5 contiguous amino acids thereof (preferably, at least 5, 10, 15, 20, 30 or 50 contiguous amino acids thereof) .
• the antibody is 1AA3.
• Antibodies can be raised to AAMP-l, or unique portions thereof, in its naturally occuring form and in its recombinant form. Binding fragments of such antibodies are also within the scope of the invention.
• AAMP-l may be joined to other materials, particularly polypeptides, as fused or covalently joined polypeptides to be used as immunogens.
• AAMP-l or its fragments may be fused or covalently linked to a variety of immunogens, such as keyhole limpet hemocyanin, bovine serum albumin, tetanus toxoid, etc. See for example.
• a typical method involves hyperimmunization of an animal with an antigen. The blood of the animal is then collected shortly after the repeated immunizations and the gamma globulin is isolated. In some instances, it is desirable to prepare monoclonal antibodies from various mammalian hosts.
• the present invention relates to a hybridoma which produces a monoclonal antibody or binding fragment thereof having binding affinity for AAMP-l.
• AAMP-l has the amino acid sequence set forth in SEQ ID NO:2, allelic or species variation thereof, or at least 5 contiguous amino acids thereof (preferably, at least 5, 10, 15, 20, 30 or 50 contiguous amino acids thereof) .
• the hybridoma comprises 1AA3.
• the present invention relates to a diagnostic kit comprising: i) at least one of the above-described monoclonal antibodies, and ii) a conjugate comprising a binding partner of said monoclonal antibody and a label.
• the present invention relates to a diagnostic kit comprising a conjugate comprising: i) at least one of the above-described monoclonal antibodies, and ii) a label.
• the present invention relates to a method of measuring the amount of AAMP-l in a sample, comprising contacting the sample with the above-described antibodies and measuring the amount of immunocomplexes formed between the antibodies and any AAMP-l in the sample.
• Methods of measuring the amount of immunocomplexes formed can be those well known in the art, such as RIA, ELISA, and direct and indirect immunoassays.
• the present invention relates to a therapeutic agent suitable for use in protecting against HIV infection or treating inflammatory immune or neoplastic disorders comprising the above-identified polypeptides in a quantity selected depending on the route of administration.
• a therapeutic agent suitable for use in protecting against HIV infection or treating inflammatory immune or neoplastic disorders
• the above-identified polypeptides in a quantity selected depending on the route of administration.
• subcutaneous or intramuscular routes of administration are preferred, the above described polypeptides could also be administered by an intraperitoneal or intravenous route.
• the amounts to be administered for any particular treatment protocol can be readily determined. Suitable amounts might be expected to fall within the range of 1-50 micromoles.
• the present invention relates to a method of using the above described polypeptide to prevent AIDS.
• the amounts to be administered for any particular treatment protocol can readily be determined.
• the present invention is described in further detail in the following non-limiting Examples.
• the selected CD4+ T-cells were free of monocytes based on the criterion that there be no proliferative response to optimal concentrations (1/200 dilution) of Phytohemagglutinin (M form) (PHA) (GIBCO, Grand Island, NY) (Davis, L., and P.E. Lipsky (1986) J. Immunol. 136:3588).
• PHA Phytohemagglutinin
• T-cell activation assays were performed using standard techniques. Briefly 10x10' purified CD4+ T-cells were cultured in 35mm flat bottom wells for various time periods in culture medium [RPMJ 1640 (Hazleton Biologies Inc. Lenexa, KS) supplemented with 20 mM glutamine (Hazleton), 10% heat inactivated FCS (Biofluids, Rockville, MD) , 100 IU/ml of penicillin, and 100 ⁇ g/ml streptomycin) ] , either unstimulated or stimulated with antibodies bound to the wells. T- cell stimulatory conditions were as described (van Seventer, G.A. et al. (1991) Eur. J.
• mAbs were immobilized on the plastic of the well by dilution in PBS and overnight incubation at 4*C, followed by washing with PBS.
• the CD3 mAb OKT3 and the CD2 mAb 95-5-49 were applied at 1 ⁇ g and 10 ⁇ g purified Ig/ml respectively, all in a volume of 3 ml/well.
• Monoclonal following antibodies were used as purified immunoglobulin derived from ascites fluid; CD2 mAb (directed against the Tll.l epitope): 95-5-49, IgGl (hybridoma kindly provided by Dr. R.R.
• RNA samples were prepared from CD4+ T cells by the guanidinium isothiocyanate-CsCl method of Maniatis et al. (Maniatis, T.E. et al. (1989) Molecular cloning: a laboratory manual. 2nd Edition. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.). 10 ⁇ g of total RNA was resolved for each condition on a formaldehyde 0.8% agarose gel, transferred to nitrocellulose, and hybridized at 42'C to M P- labeled purified AAMP-l cDNA insert prepared by random priming.
• the adaptive passive transfer technique in Balb/c mice utilizing whole cells from the human melanoma A2058 cell line as antigen was used to generate hybridomas with myeloma cells.
• Selection of the 1AA3 clone was based on its inhibition of motility when assayed in modified Boyden chambers described previously (Stracke, M.L. et al. (1987) Biochem. Biophys. Res. Comm. 146, 339-345) using gelatin coated filters and various chemoattractants (collagen type IV, laminin, autocrine otility factor, fibronectin, and insulin-like growth factor I.
• the clone 1AA3 was recloned by limiting dilution to produce the 1AA3AA clone.
• the human melanoma A2058 cDNA expression library was constructed in the lambda gtll vector by Clontech Laboratories, Inc. Y1090 Escherichia coli infected by the phage were plated and blotted onto nitrocellulose filters (Schleicher & Schnell) for immunoassay with 1AA3AA antibody. Reactive plaques were detected using peroxidase-coupled antibody specific for mouse IgG.
• Solution A (10 mM Tris Cl, pH 7.5, 0.15 MNaCl, 1.5 mM Mgclj, and 0.65% Nonidet P-40) .
• the supernate, obtained after vortexing and centrifuging (800 x G, 5 in, 4*C) was mixed with 0.8 ml Solution B (7M Urea, 1% SDS, 0.35 M NaCl, 10 mM EDTA, pH 8.0, and 10 mM Tris Cl, pH 7.5) and 1.6 ml.
• Solution C phenol: chloroform: isoamyl alcohol (50:50:1). RNA was removed in the aqueous phase and ethanol precipitated.
• Northern blots for total A2058 melanoma cytoplasmic RNA and RNA enriched for messenger RNA were performed with the Church protocol (Church, G. and Gilbert, W. (1984) Proc. Natl. Acad. Sci 81, 1991) .
• the filter was washed at 65*C for 20 minutes with wash buffer (1% sodium dodecyl sulfate, 40 mM NaH.PO., 1 mM EDTA) three times and then autoradiographed at -70'C.
• GenBank (Intel!igenetics, Inc.) was searched with the program and further analyses of the sequence was accomplished with RAOARGOS, PESTFIND, PROSITE, AACLUST, KERMIT NALIGN, PALIGN, REPEATS, SEQIN, TRANSL, AND DIAPRO programs in PC/Gene (Intelligenetics, Inc.).
• the NBRF protein sequence data base from the Protein Identification Resource National Biomedical Research Foundation (NBRF) was searched with the PQS, XQS, and NEW programs and other programs were used for sequence analyses.
• sequences are matched with a bias and gap penalty, scored in a matrix, scrambled and rescored many times to yield a mean best random score and standard deviation (SD) .
• SD standard deviation
• the score for the real sequences is expressed as the number of SD units away from the random mean score (Dayhoff, M.O. et al. (1983) Meth. Enzvm. 91, 524-545). All of our alignments were done with the Mutation Data Matrix (250 PAMs) , md, a bias of 6, a gap penalty of 6 and 150 random runs (Williams, A.F. and Barclay, A.N. (1988) Ann. Rev- yunni-no] . 6- 381-405).
• AAMP-l Antibodies The monoclonal antibody produced against AAMP-l is of the IgG-I subtype. It cryoprecipitates and loses activity with freezing and purification methods that require precipitation. Initial results indicated that this antibody inhibited adhesion and motility of A2058 melanoma cells in chemoattractant assays performed with the modified Boyden chamber. However, the inhibition occurred in an all or none fashion without a reliable dose response curve and steric hindrance due to self aggregation of the antibody cannot be ruled out at this time.
• A2058 melanoma cell surface immunofluorescent staining has been seen with . 1AA3AA. It identifies a protein on A2058 whole cell lysate immunoblots with a molecular weight of approximately 95kD that shows an apparent slight increase with reduction to 105kD.
• the betagalactosidase fusion protein shows positive staining with the 1AA3AA antibody on immunoblots.
• the predicted AAMP-l protein is described below. Its molecular weight and glycosylation potential are not consistent with the protein identified by 1AA3AA described above.
• the AAMP-l cDNA has 1766bp with the longest open reading frame (1245bp) occurring in the second reading frame of the sequence ( Figure 2; SEQ ID NO:l). 67% of the sequence excluding the poly A tail is involved with repeats that include 7 or more nucleotides each.
• the largest direct repeat is A G G A G G A A G A G at nucleotides #201 and #1685. Its sequence overlaps with that of a ten member repeat at nucleotides #197 and #1428.
• Another ten member direct repeat occurs at positions #948 and #1508 and a third 10 member repeat is at #1111 and #1171.
• the longest palindrome G G G T T C T A G A A C C C occurs at nucleotide #228. Ten member palindromes also occur at nucleotides #1149 and #1340. Eight member palindromes are present at nucleotides #228, #1119, #1515, and #1710. The last 25 nucleotides of the 1766bp sequence comprise the polyadenylated nucleotide tail and the consensus sequence A A T A A A A that commonly precedes a poly A tail is present at nucleotide #1723.
• the 1245bp open reading frame in AAMP-l cDNA predicts a protein with a molecular weight of at least 44 kilodaltons when the first methionine in the sequence (coded by the twelfth codon) is assumed to be the initiating methionine ( Figure 2; SEQ ID NO:2) .
• the predicted protein contains multiple immunoglobulin-like domains qualifying it as a member of the immunoglobulin (Ig) superfamily. It contains two potential transmembrane regions and several serine/threonine phosphorylation sites. An acidic amino terminal region is also present.
• Fourteen cysteines are present with eight present on the amino terminal side of the potential transmembrane regions (TMR) .
• Seven cysteine pairs have 57 - 78 intervening amino acids. These sizes are consistent with those found in Ig domains.
• Immunoglobulin V type domains usually have 65 - 75 intervening amino acids and C type domains have 55 - 60. Additional cysteine pairs with 43 and 44 intervening amino acids were also evaluated to find all possible domains with significant homology to the Ig domains of the superfamily members.
• AAMP-l region involving cysteines #208 and #265, aal88-285 shows significant homology with the overlapping AAMP-l region involving cysteines #208 and #265, aal88-285.
• Another region of AAMP-l involving cysteine #139 shows Ig domain homology of a lesser degree.
• Putative Ig domains with C#139 as either the first or the second cysteine forming a disulfide bond show significant Tg domain homology.
• the putative domain of AAMP-l including the aall9-228 region utilizes cysteine #139 as the first cysteine in the predicted disulfide bond.
• the other possible Ig domain involves cysteine #139 as the second cysteine in a disulfide bond and includes the region, aa79-159.
• V region domain human immunoglobulin heavy chain V-II region
• CEA PIR3:A36319
• TcR-beta V RWHUVY
• Thy-1 TDHU
• Thy- 1 membrane glycoprotein precursor
• MRC OX-2 TDRTOX V and C region domains, rat OX-2 membrane glycoprotein precursor
• CD3 epsilon PIR2:A25769
• ICAM ICAM (PIR2:S00573) domains I-V, human intercellular adhesion molecule 1; Ig kappa C (K3HU) C region domain, human immunoglobulin kappa chain C region; alpha-1-beta glycoprotein (OMHU1B) domains I and
• AAMP-l Internal Homology. Significant internal homology is also seen within AAMP-l, predominantly involving the putative Ig domains.
• the region, aall9-169, including cysteine #139 shows homology with at least three other regions containing cysteines that may or may not be involved with disulfide bonds. These are listed:
• the AAMP-l region, aa76-346, encompassing all of the potential Ig domains has predicted secondary structure characteristics consistent with what is found in Ig domains.
• the Ig fold consists of two beta sheets each containing 3-4 anti-parallel beta strands (or sheets) .
• the region, aa245-346, contains 4-8 beta sheets separated by 10 potential beta turns.
• the region, aall9-228, contains 8-9 beta sheets separated by 10 potential beta turns.
• the other two regions, aa76-159 and aa!88-228 are similar. These predictions are from the PIR CHOFAS-Protein Secondary Structure Prediction Program.
• AGC GGG GCT GCT GCT GAC ACC CCC CCA CTG GAG ACC CTA AGC TTC CAT 1 Ser Gly Ala Ala Ala Asp Thr Pro Pro Leu Glu Thr Leu Ser Phe His 10 15 20
• TCCCCTCTCC TTTTCTTCTC TTTAGAGACC CAGCCCAGGG CCCTCCCACC CTTGCCCAGA

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