Washington, D.C. 20549






November 10, 2022


Commission File Number: 001-39363




Paul-Ehrlich-Straße 15

72076 Tübingen, Federal Republic of Germany

(Address of principal executive office)


Indicate by check mark whether the registrant files or will file annual reports under cover of Form 20-F or Form 40-F:


Form 20-F

  Form 40-F


Indicate by check mark if the registrant is submitting the Form 6-K in paper as permitted by Regulation S-T Rule 101(b)(1):


Indicate by check mark if the registrant is submitting the Form 6-K in paper as permitted by Regulation S-T Rule 101(b)(7):  









On November 10, 2022, Immatics N.V. (the “Company” or “Immatics”) made available two posters, which are attached as Exhibit 99.1 and 99.2 to this Report on Form 6-K.




Exhibit No. Description
99.1 Next-Generation TCR Bispecifics (TCER) Targeting Peptide-HLA Antigens for the Treatment of Patients with Solid Tumors
99.2 The PRAME Opportunity – High Peptide Copy Numbers, Homogenous Expression and High Prevalence to Address a Broad Patient Population across Different Solid Cancers with TCR-based Therapeutics





Pursuant to the requirements of the Securities Exchange Act of 1934, the registrant has duly caused this report to be signed on its behalf by the undersigned, thereunto duly authorized.


Date: November 10, 2022  
  By: /s/ Harpreet Singh
  Name: Harpreet Singh
  Title: Chief Executive Officer




Exhibit 99.1



Next-Generation TCR Bispecifics (TCER) Targeting Peptide-HLA Antigens for the Treatment of Patients with Solid Tumors


S. Bunk1, M. Hofmann1, G. Pszolla1, F. Schwoebel1, M. Hutt1, F. Unverdorben1, N. Aschmoneit1, M. Mølhøj1, C. Wagner1, M. Jaworski1, C. Schraeder1, H. Schuster1, S. Missel1, T. Weinschenk2, D. Maurer1, C. Reinhardt2


1 Immatics Biotechnologies GmbH, Tuebingen, Germany, 2 Immatics N.V., Tuebingen, Germany










Abstract ID: 1319


Next - Generation TCR Bispecifics (TCER) Targeting Peptide - HLA Antigens for the Treatment of Patients with Solid Tumors S. Bunk 1 , M. Hofmann 1 , G. Pszolla 1 , F. Schwoebel 1 , M. Hutt 1 , F. Unverdorben 1 , N. Aschmoneit 1 , M. Mølhøj 1 , C. Wagner 1 , M. Jaworski 1 , C. Schraeder 1 , H. Schuster 1 , S. Missel 1 , T. Weinschenk 2 , D. Maurer 1 , C. Reinhardt 2 T cell engaging receptor (TCER) – a Next - generation TCR Bispecific Format • Comparison of seven different TCR bispecific formats revealed highest anti - tumor potency for TCER format together with a 2+1 format that failed specificity requirements • High affinity TCR domains targeting peptide - HLA tumor antigens are generated by specificity - controlled affinity maturation • Novel, low affinity Ab domains developed for T cell recruitment aim to improve efficacy while minimizing toxicity of TCER molecules as demonstrated in tumor xenograft models in mice and by cytokine release in human whole blood • IgG Fc region incorporated into TCER format for the extension of serum half - life and improved manufacturability • Comprehensive preclinical data package including in vivo tumor models are generated for each TCER program PRAME TCER IMA402 with encouraging preclinical and CMC data • In vivo studies in mice demonstrate dose - dependent anti - tumor activity of IMA402 and that s ufficiently high drug doses are key to achieving sustained anti - tumor response over prolonged time period • IMA402 demonstrates a serum half - life of ≈ 8 days in mice suggesting a favorable dosing regimen and prolonged drug exposure at therapeutic levels when compared to TCR bispecifics lacking half - life extension • TCER IMA402 is manufactured by utilizing standard processes of mAb production resulting in high titer , protein quality and stability while unwanted side products are absent, a unique feature of our TCER format Conclusion Pharmacodynamic and Pharmacokinetic of PRAME TCER (IMA402) Background – Overcoming Challenges of T cell Engaging Bispecifics Manufacturing of PRAME TCER (IMA402) CMC data support antibody - like manufacturability and developability • Manufacturing in Chinese Hamster Ovary (CHO) cells able to process natural TCR glycosylation • High titer (>3.5 g/L) and good stability allowing liquid formulation • Manufacturing process development completed • Manufacturing advantages of TCER format: no formation of typical but unwanted Hole - Hole and Knob - Knob side products T cell engaging bispecifics have emerged as a promising therapeutic opportunity for patients with solid cancers . However, challenges related to target specificity and drug safety remain and many efforts are being made to generate optimized molecules with improved pharmacodynamics while reducing T cell engager - associated toxicities . We have developed a pipeline of bispecific T cell engaging receptor (TCER) molecules comprising a T cell receptor (TCR) for giving access to intracellular tumor antigens presented as peptide - HLA molecules . The next - generation design of TCER is established through a novel, low - affinity T cell recruiting antibody aiming at conferring a favorable drug safety profile while enabling a highly potent anti - tumor response . TCER molecules are further equipped with an effector function - silenced Fc region for prolongation of serum half - life . Target - unrelated cytokine release in human whole blood is reduced with low - affinity recruiter Abstract ID: 1319 1 Immatics Biotechnologies GmbH, Tuebingen, Germany, 2 Immatics N . V . , Tuebingen, Germany TCER IMA402 TCER - Ab1 TCER - Ab3 INF γ IL - 6 IL - 8 TNFα TCER [µg/ml] TCER [µg/ml] TCER [µg/ml] TCER [µg/ml] Figure 3 . Whole blood cytokine release assay to assess the risk of different recruiters to induce cytokines in absence of target . Recruiter arm - driven non - specific activation of T cells was assessed by measuring TCER - mediated cytokine release in whole blood of 3 HLA - A* 02 - positive donors and human endothelial cells (HUVEC) after incubation with PRAME TCER IMA 402 , TCER - Ab 1 or TCER - Ab 3 for 48 h . N = 16 cytokines tested, individual values for 4 exemplary cytokines shown . Higher background of IL - 6 is due to the presence of HUVEC . TCER - Ab 2 was not tested . Contact information: info@immatics.com Discovery and Affinity Maturation of TCRs Required for TCER Generation *high potency of 2+1 format D was caused by pronounced unspecific reactivity against T2 Killing of target - positive tumor cells by different TCR Bispecifics TCER Format Exhibits Highest Potency Combined with Specificity in Targeting pHLA Antigens TCER T cell recruiting antibody pHLA targeting TCR Fc region (silenced) with KiH technology High affinity (single digit nM ) TCR targeting tumor - specific peptide HLA molecules Low affinity (triple digit nM ) T cell recruiter against CD3/TCR Human IgG Fc region (silenced) with knob - in - hole technology for half - life extension, favorable stability and manufacturability Proprietary TCER format consisting of three distinct elements designed for optimal efficacy and minimal toxicity risk in patients Cytotoxic lytic granules T umor cell A ctivated T cell TCER binds to target, recruits and activates T cells and initiates tumor cell killing 2 1 3 The Next - generation of TCR Bispecifics – TCER Preclinical Data Package for TCER Programs Widely used T cell recruiting Ab (3 variants) medium to high affinity (single to double digit nM ) Immatics’ T cell recruiting Ab low affinity (triple digit nM ) TCER molecules are designed with a high affinity TCR and a low affinity T cell recruiting Ab to optimize biodistribution * . The design also intends to selectively induce T cell activation at the tumor site but not in the periphery and thereby reducing immune - related toxicities, like cytokine release syndrome, and to reach sufficiently high drug doses for achieving meaningful clinical responses . Figure 2 . In vivo efficacy assessment of TCER molecules incorporating identical tumor - targeting TCR domains, but different T cell recruiting Ab domains in Hs 695 T (melanoma) cell line xenograft model in NOG mice . Weekly intravenous injections of 0 . 025 mg/kg body weight of PRAME - specific TCER molecules for three weeks starting at study day 1 after intravenous transfusion of human PBMC . PRAME TCER IMA 402 utilizes a novel, low affinity recruiter ( triple digit nM affinity) binding both CD 3 and TCR . Analogous TCER molecules TCER - Ab 1 , - Ab 2 and - Ab 3 utilize medium to high affinity recruiters (TCER - Ab 1 : 39 nM , TCER - Ab 2 : 9 nM , TCER - Ab 3 : 31 nM ) binding CD 3 only . Novel, Low - Affinity Recruiter Designed to Improve Efficacy/Toxicity Profile of TCER n = 6 mice/treatment group, n = 10 mice in vehicle group, 2 donors/group Superior tumor control using a novel, low - affinity recruiter with high T cell activation capacity * R efer to literature data for other low - affinity recruiters (e.g. Harber et al ., 2021, Nature; Trinklein et al ., 2019, mAbs ) A B C D E F D* TCER A C B E F • TCR variable domains ( scTv format) are stabilized and optimized for facilitated production in mammalian cells • This enables combination with various bispecific platforms • Low binding affinity of natural TCRs is increased by at least 1,000 - fold while retaining high specificity • XPRESIDENT’s immunopeptidome database is essential for specificity - controlled affinity maturation • XCEPTOR for TCR Discovery, Engineering & Validation • Generation of multiple TCR candidates per target • Unique XPRESIDENT - guided on - and off - target toxicity screening Figure 4 . In vivo efficacy of IMA 402 in large ( ≈ 195 mm 3 average tumor volume ) melanoma cell line - derived tumors in MHC I/II knock - out NSG mice over a prolonged observation period of 71 days . Weekly intravenous injections of IMA 402 starting at study day 1 after intravenous transfusion of human PBMC . Treatment was discontinued when complete response was noted . Median values for n = 6 mice/group, 2 donors/group . Figure 5 . Pharmacokinetic analysis of IMA 402 in mice . NOG mice received a single intravenous injection of IMA 402 ( 2 mg/kg) . TCER plasma concentrations at different time points were determined by ELISA detecting binding of IMA 402 to the PRAME target via pHLA . The integrity of the molecule was confirmed via aV L or aFc detection . Terminal half - life (t 1 / 2 ) was calculated via linear regression of time points between 24 h and 360 h (n= 3 per timepoint, mean ц SD) . Figure 1 : Design and cytotoxic activity of TCER and six alternative TCR bispecific formats . Right panel : Based on an affinity - maturated TCR (TCR variable domains in red) specific for the HIV peptide SLYNTVATL presented on HLA - A* 02 , TCER and six alternative TCR bispecific formats were generated using the identical Fab region for T cell recruitment (variable Ab domains in blue) . Silenced IgG 1 Fc domains with knob - into - hole ( KiH ) were utilized to facilitate heterodimerization . ​ Left panel : PBMC - mediated cytotoxicity of TCR bispecific formats against HLA - A* 02 – positive T 2 cells loaded with HIV peptide . Cytotoxicity was calculated based on LDH release during 24 h coculture of PBMC and T 2 . LDH content of T 2 cells alone was used as 100 % cytotoxicity reference leading to underestimated cytotoxicity values due to T 2 cell proliferation . Figure 6 . Theoretical product - related impurities such as hole - hole and knob - knob homodimers, are considered inactive due to absence of variable IgG or TCR domains . Total mass analysis by mass spectrometry ( MS) of transiently and CHO stably expressed IMA 402 has demonstrated lack of hole - hole and knob - knob homodimers in both Protein - L and Protein - A captured TCER fractions . IMA 402 was analyzed by MS after complete deglycosylation with PNGase F . With a 100 % correct chain pairing of the TCER knob and hole chains, IMA 402 can be captured with standard Protein - A chromatography, and n o specific downstream processing steps are needed for the removal of these product - related impurities . Detected by MS Not detected by MS • XPRESIDENT data package • Absolute quantification of target pHLA copies ( AbsQuant ) • Homogeneity of target pHLA presentation within tumors • Tumor cell lines presenting target pHLA at endogenous levels • Tumor cell - mediated cytokine release and proliferation of T cells • Tumor xenografts in mice • Pharmacokinetic and - dynamic • Normal tissue cell types and iPSC - derived normal cells (n≥20) • Target - negative tumor cell lines • Alloreactivity screening • Cytokine release from whole blood • XPRESIDENT - guided off - target screening based on similarity to target peptide sequence and TCR binding motif • Yield and purity of material produced by CHO cells • Freeze - thaw and storage stress stability • Sequence liabilities • N - glycan profiling of TCR domains Target Validation Assessment of Efficacy Assessment of Safety & Specificity Manufacturability Developability V α VL VH V β V α VL VH V β MW aver., SS , Δm = +0 Da Mass Intensity Hole - Hole Knob - Knob TCER: 100% correct chain pairing V α V α VH VH VL VL V β V β Hole chain Knob chain PNGase F digest Knob - Hole TCER

Exhibit 99.2


The PRAME Opportunity – High Peptide Copy Numbers, Homogenous Expression and High Prevalence to Address a Broad Patient Population across Different Solid Cancers with TCR-based Therapeutics


J. Hukelmann1, C. M. Britten2, D. Araujo3, L. Backert1, C. Bokemeyer4, R. Caravajal5, M. Chatterjee6, A. Dash7, L. Freudenmann1, J. Fritsche1, D. Fuhrmann1, V. Goldfinger1, T. Holderried8, F. Hoffgaard1, A. Jazaeri3, A. Kaseb3, F. Köhler1, D. Kowalewski1, J. Luke9, V. Morris3, S. Mukhi7, M. Ott1, R. Reshef5, M. Römer1, L. Rostock1, S. Satam1, A. Satelli7, C. Schräder1, M. Thambi7, A. Tsimberidou3, M. Wagner1, M. Wermke10, H. Schuster1, O. Schoor1, T. Weinschenk2


1 Immatics Biotechnologies GmbH, Tuebingen, Germany, 2 Immatics N.V., Tuebingen, Germany, 3 MD Anderson Cancer Center, Houston, Texas, USA, 4 University Medical Center Hamburg-Eppendorf, Germany,, 5 Columbia University, New York, USA, 6 University Hospital Würzburg, Germany, 7 Immatics US, Inc., Houston, Texas, USA, 8 University Hospital Bonn, Germany, 9 University of Pittsburgh, Pittsburgh, Pennsylvania, USA, 10 University Hospital Dresden, Germany




Abstract ID: 713








Abbreviations: adipose: adipose tissue; adrenal gl: adrenal gland; bloodvess: bloodvessel; esoph: esophagus; gall bl: gallbladder; intest. la: large intestine; intest. sm: small intestine; nerve periph: peripheral nerve; parathyr: parathyroid gland; perit: peritoneum; pituit: pituitary; skel. mus: skeletal muscle; thyroid: thyroid gland; AML: acute myeloid leukemia; BRCA: breast cancer; CCC: cholangiocellular carcinoma; CLL: chronic lymphocytic leukemia; CRC: colorectal cancer; GBC: gallbladder cancer; GBM: glioblastoma; GC: gastric cancer; GEJC: Gastro-esophageal junction cancer; HCC: hepatocellular carcinoma; HNSCC: head and neck squamous cell carcinoma; MEL: melanoma; MPNST: malignant peripheral neve sheath tumor; NHL: Non-Hodgkin lymphoma; NSCLCadeno: non- small cell lung cancer adenocarcinoma; NSCLCother: NSCLC samples that could not unambiguously be assigned to NSCLCadeno or NSCLCsquam; NSCLCsquam: squamous cell non-small cell lung cancer; ORR: objective response rate; OC: ovarian cancer; OSCAR: esophageal cancer; PACA: pancreatic cancer; PRCA: prostate cancer; RCC: renal cell carcinoma; TNBC: triple-negative breast cancer; SCLC: small cell lung cancer; UBC: urinary bladder carcinoma; UEC: uterine and endometrial cancer. 



The PRAME Opportunity – High Peptide Copy Numbers, Homogenous Expression and High Prevalence to Address a Broad Patient Population across Different Solid Cancers with TCR - based Therapeutics Clinical Validation of PRAME as Multi - Tumor Target for TCR - based Therapies Acknowledgements : We are immensely grateful to the patients and their families . Contact information: info@immatics.com PRAME – Promising Opportunity for TCR - based Therapies Several peptide - HLA targets for T cell receptor (TCR) - based immunotherapies are currently being evaluated in the field, however, many are limited by their overall low prevalence, low copy numbers or relevant expression in healthy tissues . A T cell target with nearly ideal properties has high, homogenous and prevalent expression across multiple cancers in the absence of significant safety/toxicity liabilities . Here, we describe the in - depth characterization of an HLA - A* 02 : 01 - presented peptide derived from the cancer germline antigen preferentially expressed antigen in melanoma (PRAME) that opens an avenue of new opportunities for patients with solid cancers which we aim to leverage by two distinct TCR - based therapeutic modalities, TCR - engineered T cells ( ACTengine IMA 203 ) and TCR Bispecifics (TCER IMA 402 ) . PRAME Expression is Highly Cancer - Associated Bringing Two Distinct TCR - based Modalities to Cancer Patients by Targeting PRAME Figure XX . XXXXX PRAME Is Homogenously Expressed across Different Solid Tumors • PRAME RNA expression is elevated across multiple different solid tumor types • Stable PRAME RNA expression across early and late tumor stages and tumor subtypes • Minimal expression in some normal tissues except testis, not translating into relevant peptide presentation (see Figure 4) Proprietary Technologies to Analyze PRAME on Every Cellular Level Abbreviations : adipose : adipose tissue ; adrenal gl : adrenal gland ; bloodvess : bloodvessel ; esoph : esophagus ; gall bl : gallbladder ; intest . la : large intestine ; intest . sm : small intestine ; nerve periph : peripheral nerve ; parathyr : parathyroid gland ; perit : peritoneum ; pituit : pituitary ; skel . mus : skeletal muscle ; thyroid : thyroid gland ; AML : acute myeloid leukemia ; BRCA : breast cancer ; CCC : cholangiocellular carcinoma ; CLL : chronic lymphocytic leukemia ; CRC : colorectal cancer ; GBC : gallbladder cancer ; GBM : glioblastoma ; GC : gastric cancer ; GEJC : Gastro - esophageal junction cancer ; HCC : hepatocellular carcinoma ; HNSCC : head and neck squamous cell carcinoma ; MEL : melanoma ; MPNST : malignant peripheral neve sheath tumor ; NHL : Non - Hodgkin lymphoma ; NSCLCadeno : non - small cell lung cancer adenocarcinoma ; NSCLCother : NSCLC samples that could not unambiguously be assigned to NSCLCadeno or NSCLCsquam ; NSCLCsquam : squamous cell non - small cell lung cancer ; ORR : objective response rate ; OC : ovarian cancer ; OSCAR : esophageal cancer ; PACA : pancreatic cancer ; PRCA : prostate cancer ; RCC : renal cell carcinoma ; TNBC : triple - negative breast cancer ; SCLC : small cell lung cancer ; UBC : urinary bladder carcinoma ; UEC : uterine and endometrial cancer . In - house multi - dimensional quantitative analysis of tumor & normal tissues, cell lines, CDX and PDX models Protein mRNA Peptide PRAME peptide - HLA complex • HLA - A*02:01 - presented PRAME peptide for development of TCR - based therapies selected among >30 possible PRAME - derived HLA - A*02:01 peptides • Mass spectrometry (MS) and matched RNAseq data from healthy normal and tumor samples were processed and organized into a large quantitative immuno - peptidomics database using proprietary immunoinformatics platform XCUBE • Based on matched RNAseq and MS data, we defined an RNA threshold which corresponds to actual peptide presentation (Fritsche et al. , 2018). This MS - guided RNA threshold is used for • clinical patient stratification • prevalence estimation RNA level • RNA sequencing to analyze tumor - specificity • ISH to analyze target homogeneity • qRT - PCR: IMADetect biomarker assay for clinical patient stratification Protein level • Mass spec - based proteomics to assess target and HLA protein levels Peptide level • Mass spec - based relative target peptide levels • Mass spec - based absolute target peptide copies per cell ( AbsQuant ) Figure 1 . Immatics’ XPRESIDENT - based multi - dimensional analysis of PRAME . • HLA - A*02:01 - presented PRAME peptide can be measured directly via mass spectrometry in over 20 solid and liquid tumor entities • PRAME RNA expression does not translate into relevant presentation on healthy normal tissues • Quantification using Immatics’ highly sensitive AbsQuant technology reveals PRAME target density of 100 - 1,000 copies per cell in tumor tissues Figure 4 . HLA* 02 : 01 - presented PRAME relative presentation levels on HLA - A* 02 positive normal and tumor tissues quantified via MS . Each dot represents the median PRAME pHLA - derived MS intensity as an indicator for target abundance in one sample . Box - and - whisker plots represent signal intensities of multiple samples per organ or tumor entity . 100 µm Healthy normal tissue Cancer tissue Figure 5 . S patial expression of PRAME analyzed by in situ hybridization (ISH) in various tumor types ( NSCLCsquam , NSCLCadeno , OC, UEC, HNSCC) . Representative images from two patients per tumor type . Positive signal intensity is visualized as red dots or clusters of red dots using Fast Red . Nuclei are stained with haematoxylin . Scale bar 100 μm . • In situ hybridization was used to analyze PRAME expression homogeneity in several solid tumor samples • Histologic analysis of PRAME RNA in different solid tumors demonstrates homogenous expression of PRAME with a high frequency of positive tumor cells Immatics’ mass spectrometry - guided RNA threshold 95% 50% 2 100% 80% 100% Up to 100% 65% 60% 55% Up to 45% 35% 25% 25% 25% 20% 20% 20% 1 XPRESIDENT XCEPTOR Adoptive Cell Therapies TCR Bispecifics ACTengine IMA203 TCER IMA402 Discovery & Validation of Targets Identification & Engineering of TCRs Generation, Characterization & Validation of Product Candidates Clinical Trials PRAME peptide - HLA c omplex Tumor cell TCR Technology Platforms Foundation of Deep Know - how Two Distinct Modalities Targeting PRAME Delivering the Power of T cells to Cancer Patients Figure 3 . PRAME exon expression based on in - house RNA sequencing data . Expression of all exons encoding the PRAME target peptide in normal tissues from various organs and in different hematologic and solid cancer types . Each dot represents the maximum TPM value across all peptide - encoding exons in one sample . Box - and - whisker plots represent TPM values of multiple samples per organ or tumor entity . TPM : transcripts per million . PRAME Peptide Is Presented across Multiple Tumors Abstract ID: 713 % PRAME positive patients 1 Patient screening data obtained via IMADetect biomarker assay in Immatics’ clinical trials support high prevalence of PRAME Cutaneous Melanoma 95% Uveal Melanoma 2 90% Uterine Carcinoma 90% Ovarian Carcinoma 70% Figure 6 . PRAME target expression and prevalences in selected solid cancer types based on in - house and TCGA data (https : //www . cancer . gov/tcga ) . 1 PRAME target expression and prevalence based on TCGA (for SCLC : in - house) RNAseq data combined with a proprietary MS - guided RNA expression threshold ; 2 TCGA : early & late - stage primary tumor samples, Immatics clinical trials : late - stage/metastatic tumor samples ; Role of PRAME in metastasis of uveal melanoma : Field et al . 2016 Clinical Cancer Research Here, we demonstrate comprehensive target characterization and validation data supporting the favorable target properties of PRAME that can be exploited for the benefit of patients . Preclinical data of PRAME show that the target is • highly cancer - associated, • presented at high target density, • homogenously expressed and • highly prevalent across many solid cancers underlining its potential to reach a large cancer patient population . The data obtained during the ongoing Phase 1 trial provide clinical validation of PRAME as a highly promising T cell target for solid cancers . Confirmed clinical responses were observed at all PRAME - expression levels above threshold, indicating IMA 203 ’s potential to provide clinical benefit for all PRAME biomarker - positive cancer patients with tolerable adverse events . The predicted high PRAME prevalence across key indications has so far been supported by prevalence rates obtained during the clinical screening of patients . Figure 2 . Immatics’ approach to develop TCR - based product candidates for cancer patients . Healthy normal tissue Cancer tissue Conclusions • High clinical activity of IMA203 TCR - T: 50% (6/12) confirmed objective response rate ( cORR ) in patients with at least 1 billion infused TCR - T cells across Phase 1a and 1b; thereof 80% cORR (4/5) in Phase 1b patients alone with all responses ongoing at data cut - off* • Most frequent treatment - emergent adverse events (TEAEs) were cytopenia, cytokine release syndrome, and grade 1 and 2 immune effector cell associated neurotoxicity syndrome. The TEAE profile is acceptable and adverse events were manageable • Confirmed responses across different solid tumor types: cutaneous melanoma, ovarian cancer, head and neck cancer, uveal melanoma, and synovial sarcoma Figure 7 . ACTengine IMA 203 TCR - T targeting PRAME . For application as TCR - engineered T cell therapy (TCR - T) approach, the IMA 203 PRAME TCR is engineered via lentiviral transduction into a patient Dz s own T cells whose tumor has been tested positive for PRAME . The TCR - T cells are designed to bind to the PRAME pHLA target to induce a robust and specific anti - tumor response to fight the cancer . * Immatics ACTengine ® IMA 203 TCR - T Targeting PRAME Monotherapy Interim clinical Data Update on Oct 10 , 2022 (data cut - off Sep 6 th , 2022 ) Clinical validation of Immatics’ mass spectrometry - guided RNA threshold for PRAME: Confirmed responses were observed at high and low PRAME - expression levels above the threshold J . Hukelmann 1 , C . M . Britten 2 , D . Araujo 3 , L . Backert 1 , C . Bokemeyer 4 , R . Caravajal 5 , M . Chatterjee 6 , A . Dash 7 , L . Freudenmann 1 , J . Fritsche 1 , D . Fuhrmann 1 , V . Goldfinger 1 , T . Holderried 8 , F . Hoffgaard 1 , A . Jazaeri 3 , A . Kaseb 3 , F . Köhler 1 , D . Kowalewski 1 , J . Luke 9 , V . Morris 3 , S . Mukhi 7 , M . Ott 1 , R . Reshef 5 , M . Römer 1 , L . Rostock 1 , S . Satam 1 , A . Satelli 7 , C . Schräder 1 , M . Thambi 7 , A . Tsimberidou 3 , M . Wagner 1 , M . Wermke 10 , H . Schuster 1 , O . Schoor 1 , T . Weinschenk 2 , 1 Immatics Biotechnologies GmbH, Tuebingen, Germany, 2 Immatics N.V., Tuebingen, Germany, 3 MD Anderson Cancer Center , Houston, Texas, USA, 4 University Medical Center Hamburg - Eppendorf, Germany, , 5 Columbia University, New York, USA, 6 University Hospital Würzburg, Germany, 7 Immatics US, Inc., Houston, Texas, USA, 8 University Hospital Bonn, Germany, 9 University of Pittsburgh, Pittsburgh, Pennsylvania, USA, 10 University Hospital Dresden, Germany