3101 LPSAGRGVCYEA QHLNSILLVTK YPHGYVAFGRW 3 Phage display (competitive panning) 3 PMID:27766741 Anti-LPS single-domain antibody fragment VHH lipopolysaccharide, LPS Not determined. Not determined. Ph.D.-12 phage display library (X12) ELISA The binding activities of phage clones to the VHH were measured by phage ELISA. The OD values at 490 nm were measured and data shown were reproduced from the Fig. 2A in the reference. Bound phages were eluted with 100μl elution buffer. In order to compete with the immobilized VHH on the plate, the elution buffer was added VHH in a concentration of 100μg/ml. 3102 EMFTPPSMIERL 1 Phage display (in vivo) 2 PMID:27768975 Ocular tissues Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) The Ph.D.-12 library was topically applied into the conjunctival sac or injected into the retrobulbar space of male Sprague-Dawley rats. One hour after administration, aqueous humor was extracted, the eyes were enucleated, and the iris, vitreous humor, retina and choroid were dissociated after washing. A novel dodecapeptide with the sequence of EMFTPPSMIERL, named CC12, was identified with the ability to penetrate the ocular barrier in a noninvasive (via conjunctival sac instillation) or minimally invasive (via retrobulbar injection) manner. KV11, an antiangiogenesis peptide previously demonstrated to inhibit pathological neovascularization in the retina, was then used as a model antiangiogenesis cargo for CC12. It was found that conjugation of KV11 peptide with CC12 peptide facilitated the delivery of KV11 to the retina, resulting in significant inhibition of retinal neovascularization development via topical application without tissue toxicity. 3103 CRGATPMSC(5) CTHLRHASC(4) CMSTGLSSC(3) CGGGPLYMC(2) CSQLPWYSC(1) CPNSTHRNC(1) CPTVKQKWC(1) CNMFDARAC(1) CNPSKEKTC(1) CLMTSQFRC(1) CTRGDRIPC(1) CYENTRHTC(1) CNTGSPYEC(1) CDKVESRVC(1) CKNLSHEPC(1) CQQLTHADC(1) CPTTVGIKC(1) CLKDRIPLC(1) CPLQNSPTC(1) CSIKSKPSC(1) CNNKFLANC(1) CRMNSLLDC(1) CVPSRMEKC(1) CSSDTDKTC(1) CTPFLGRLC(1) CPSWYKNEC(1) CDESKVQTC(1) CSLASAATC(1) CIATSKPSC(1) CTQTGDMAC(1) CAEFTVAGC(1) CLGPGGFSC(1) CEHTANSLC(1) CLQKTYPQC(1) CLYSTKTMC(1) CDAPMKYMC(1) CSSTYLNLC(1) CLNTNTMSC(1) CGNNGNNTC(1) CDELHNAAC(1) 40 Phage display (common panning) 3/4 PMID:27802020 Tetragonal Barium Titanate (BaTiO3 or BT) Nanocrystals Not determined. Not determined. Not determined. Ph.D.-C7C phage display library (CX7C) After the third round of selection, 50 random colonies were picked out separately for DNA sequencing A short BaTiO3-binding/nucleating peptide, CRGATPMSC (named RS), was identified. We found that the resultant phages could not only bind with the presynthesized BaTiO3 crystals but also induce the nucleation of uniform tetragonal BaTiO3 nanocrystals at room temperature and without the use of toxic reagents to form one-dimensional polycrystalline BaTiO3 nanowires. This approach enables the green synthesis of BaTiO3 polycrystalline nanowires with potential applications in bioimaging and biosensingfields. 3104 CLGTTPFFC(4)[1.52, 16.9] CLYHPWNNC(3)[1.41, 20.1] CTGTTPFYC(3)[1.64, 12.6] CRGSMPFWC(3)[1.38, 18.4] CMARYMSAC(2)[1.59, 13.2] 5 Phage display (common panning) 3 PMID:27874102 Anti-OPs monoclonal antibody mAb3C9 O,O-dimethyl organophosphorus pesticides (O,O-dimethyl OPs) Not determined. Not determined. Ph.D.-C7C phage display library (CX7C) ELISA The binding activities of phage clones to the mAb3C9 were measured by phage ELISA. The absorbance was recorded at 450 nm. The affinity data in the first column are the maximal absorbance, while the affinity data in the second column are the IC50 (ng/mL). 3105 CPHPQRPAC[0.21] CKIMKASPC[1.00] CASACPPHC[1.33] CGLHKVHKC[0.83] CHEQKSLPC[0.67] CKSSSVLWC[1.22] CLPGKHGHC[3.41] CTSHPRPSC[4.15] CSVTTHLLC[2.01] SKIVSTPSC[2.20] CMLNSKHYC[2.23] CFHLPSTYC[2.01] 12 Phage display (common panning) 2-4 PMID:277290620 Interleukin-7 receptor subunit alpha, IL-7RA Not determined. Not determined. Not determined. Ph.D.-C7C phage display library (CX7C) ELISA The binding activities of phage clones to the IL-7Rα were measured by phage ELISA. The OD values at 405 nm were measured. The data shown are the apparent dissociation constant values (Kd, nM). The phage library was pre-panned against the Dynabeads free of protein but blocked with BSA, Fc/IgG-coated Dynabeads and fibronectin coated well before selection agaist IL-7Rα-coated Dynabeads® Protein A or G. 3106 LWWQIWDG(4) PWWWGRNV(3) WIWAWRSS(1) LSWWSRKW(1) WWAIWMQE(1) 5 Phage display (common panning) 2 PMID:27756316 Coxsackievirus A9 lacking the RGD motif (CV-A9-RGDdel) Not determined. Not determined. Not determined. CX8C phage display library 3107 KFPDIDSISSLW(3) STDSIITNSQRL(2) FEDSIVSTRETF(1) YYDDTASIRSSR(1) VNLSDLSLHYPS(1) SGVYKVAYDWQH(1) HTEDDTASITTS(1) DRSSDSIVSWRG(1) AYAGSTGLFERG(1) NFSPSNVPGDKF(1) HVDTGSDKKLDH(1) SDSDSIRTYMNI(1) RSEGEVLSPETL(1) DSISSIVTSQAF(1) MDGLDSIYTSSR(1) GQIIQDFDWVQN(1) SSTDSIMSSYIG(1) ACCDIDSIKSSV(1) 18 Phage display (common panning) 3 PMID:28072528 Anti-Dengue virus (DENV) polyclonal antibody Triosephosphate isomerase (TIM) Not determined. Not determined. Ph.D.-12 phage display library (X12) 3108 RGWGNGCGLF GDQHQVGNET MDFNEMILLT MPLPWTSGAT LPWTSGATTE MGSQEGAMHT SQEGAMHTAL QEGAMHTALT LTGATEIQNS MKKEVSETQH TEDGQGKAHN KGSSIGKMFE MNSKNTSMSF MLWKQIANEL MTVVVGDIIG MMSAAVKDER MAGPISQHNH MVSAGSGKVD YKKGSSIGKMFE LKYSWKTGKAK 20 Phage display (common panning) 2 PMID:28152075 Anti-Dengue virus (DENV) polyclonal antibody Dengue virus (DENV) Not determined. Not determined. Bacteriophage MS2 VLP DENV-3 antigen fragment library ELISA We utilized a pathogen-specific antigen fragment library displayed on bacteriophage MS2-VLPs in combination with deep sequence-coupled biopanning. 3109 RDYHPRDHTATWGGG(1)[0.47857±0.01259] ISSFGNPEFSTGGG(2)[0.03014±0.00254] NYPWMAGTQSMGGG(3) [0.02168±0.00255] GNNPLHVHHDKRGGG(4)[0.34423±0.03388] SHTFVNEHTPPSGGG(5)[0.03148±0.00254] WLDDQTMRNLDSGGG(6)[0.03777±0.00496] SPLRAVAFSGAQGGG(7)[0.03643±0.00375] GADTSKPPRFVTGGG(8)[0.02518±0.02264] VCSPCGPVPPAKGGG(9)[0.04527±0.00121] HMYYPGGDGRFAGGG(10)[0.04648±0.01513] 10 Phage display (subtractive panning) 3 PMID:28186164 NIST RM8670 (NISTmAb) Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) Absorbance was read at 450 nm. The Absorbance values shown were regenerated from Figure 2 in the published paper. Phage display panning was performed in a subtractive manner. The library was initially depleted with control non-aggregated NISTmAb using three iterative cycles.The unbound phage was then screened on cross-linked NISTmAb aggregates, again using three iterative cycles of phage binding, elution, and amplification. Peptides RDYHPRDHTATWGGG and GNNPLHVHHDKRGGG possess preferential binding to NISTmAb aggregates. 3110 WBRMPAYTAKYP WBRMPMETAKPL KNPTSTPAMYAN KPPQBTSAPYLP GBRNRANTSKNP GHWHSPHKLTRN RxPxxTxK 6 Phage display (common panning) 5 PMID:28220894 GST-N1-Src SH3 domain Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) By screening a peptide phage display library, we discovered a novel ligand (WHRMPAYTAKYP, PDN1) that targets the unique SH3 domain of N1-Src and inhibits N1-Src in cells. In cultured neurons, PDN1 fused to a fluorescent protein inhibited neurite outgrowth, an effect that was mimicked by shRNA targeting theN1-Src microexon. PDN1 also inhibited L1-CAM-dependent neurite elongation in cerebellar granuleneurons, a pathway previously shown to be disrupted in Src−/− mice. PDN1 therefore represents anovel tool for distinguishing the functions of N1-Src and C-Src in neurons and is a starting point for the development of a small molecule inhibitor of N1-Src. 3111 EWWWW 1 Phage display (common panning) 2 PMID:28315327 Kelch-like ECH-associated protein 1 Nuclear factor erythroid 2-related factor 2 Not determined. Not determined. X4 T7 phage display library Biotinylated Avi-tagged Keap1 Kelch domain was immobilized to Dynabeads M280-streptavidin (Invitrogen) in PBS (045e29795, Wako) containing 0.5% BSA. After washing the beads using PBS containing 0.1% Tween 20 (PBST), the beads were incubated with the phage libraries for 1 h and were washed with PBST. The bound phages were eluted with 0.5% SDS and were incubated with E. coli BLT5615 cells (Merck Millipore) in log-phase growth for phage amplification. After bacteriolysis, the phages were recovered from the culture supernatant by centrifugation and PEG-precipitation according to manufacturer's T7 protocol. The recovered phages were suspended in PBS and were used for the next round of panning. We identified a tetrapeptide, EWWW, showing moderate binding affinity, which inhibits the interaction between Nrf2 and Keap1. The tetrapeptide does not include an ETGE motif, which is a commonly found consensus sequence in known peptidic inhibitors. In addition to affinity parameters, IC50, KD, and thermodynamic parameters, the crystal structure of the complex was determined to elucidate the binding conformation. The binding interactions resemble those of known small-molecule inhibitors as opposed to those of substrates and peptidic inhibitors. 3112 ANKNLLFKIRYSTAR 1 Phage display (common panning) 5 PMID:28254693 Toll-like receptor-4 (TLR4) and myeloid differentiation factor 2 (MD2) complex Not determined. Not determined. Not determined. X15 fUSE55 phage display library 3113 LDCFRWGWRMWC YEIRCWWRWCYT 2 Phage display (common panning) 5 PMID:28254693 Toll-like receptor-4 (TLR4) and myeloid differentiation factor 2 (MD2) complex Not determined. Not determined. Not determined. X12 pHEN2 phage display library 3114 HINWPILPRLWV SPDHASRDWRSR TQLDDHKRSHHA ISRPTPSVNPLM LTQGTSDMTRHL SWKPYTWKDTAL FQGSPKTNHGKI GPTFNLQRIPAT QTKSSVYMMSYL WHSNNSHNDSWP ADKPRVDTTTYN IRLPASLLLDPA GPKSNNVGVTYS FWPHKHNLYMST AHWFGGVYNKTM TPLPSPIDITYQ YALHDGTAHNTW LQASAKTMHGTI SNTYLPKSYLNV AHRYIDAQIDRR SMLRQEFPPTEP QTHHHTFFMKSK YYYADDGAILLN 23 Phage display (common panning) 3 PMID:28184219 Anti-E. rhusiopathiae polyclonal antibodies Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) Solid phase panning was applied for the first round of biopanning. Solution-phase panning by the affinity SPA Sepharose capture method was applied for second round biopanning. 3115 CMSLLTATC CDLKSTVKC CNNWLTMPC CNTVRESVC CVSRYNWGC CSHNQPYQC CLQAKPRTC CLSKWTTSC CLNANTSLC CSPNYSRNC CNADKPTEC CERTNSSDC CQPSRDTYC CYGDSNLAC CGQEGMKEC CNAMLRAVC CLPFMIHNC CILSDSGSC CPTVKQKWC CSSATLVYC CGAKWMSQC CRDKALVNC CNTTQSVMC CSTSFDNSC CLALDRRDC CYRPTTDQC CLKTLNPSC CQYRNHADC CSFPKNLDC CFQPKRLDC CSSSGQRLC CYRENHSYC CILNYPESC CQEGTNKAC 34 Phage display (common panning) 3 PMID:28184219 Anti-E. rhusiopathiae polyclonal antibodies Not determined. Not determined. Not determined. Ph.D.-C7C phage display library (CX7C) Solid phase panning was applied for the first round of biopanning. Solution-phase panning by the affinity SPA Sepharose capture method was applied for second round biopanning. 3116 NPVEDYLDYSVI ESYYMNPVEMFV LPTESNPVEDWI NPIESYIASVFS NPVELLLKTSSD NPVETQIVLSLV NPVEKWISMRTM NPVELLLLMGIS NGIERLLEEPVS NPVENWIDPKSI VNPVEYYLDTMR NPVEALLSKFHM NPVESYLANYTS VTNPYESLVQEK SPPEFSGSTVGL MVPEFSGSFPMR RMPPEFMGSLPQ QLFVPEFAGSSP LVPEFTGSTPFR SHGAIEFDGAFP VPEFAGHVPSTA VPEMNGSLIARK HPIVKTYFAQTT APAKTYFGQTTD QMKAWFPQTTYD ATKVMFPQRIYV QPAKTYFNQVTL QAAAKTMFPQNT SPSIDAFETSIF SWVLTATETGSS EMRFPSLSASDT QAPTLDAQETAL TALDAVSTGFSW GAIGSLTADSTS SLGSLSAYETGR TLYRPPLTSAET LIADLNAESTSR SLGAAGARVTTV ASGPLHAGATGL GHKPVLTALSTA VMPAIHAGVTGA VHPTLTVTSKEI ELDVSLRVMPKV SKLAMEIMSGPV SNAVTSSKSPRM QADATVLTKPKT KAVSDASRGTVF DYPKIANFQEYA GGQVRSIHSGPT QHWPTNVDSVTV ETKSDDMLLSNV MTVDRTVRVASK DLLIRDAITDTK AYHVDTVSDAGW VDTINLPQNTIQ VMSVNASTTAAN TLHAPMTIRSGP TNLHRVMTVVNM LRPNAVQTDTLA QMRQLTEYGSEK VLSSTAIKVDSV VHTVHDVFTAFG AKIRMFLDTDYK ASWGPIAIDRVN SQQYALTNSTTN QPQTKSFYPQYV NVVDRVNRTGVV WSALPERTSLPV RPAIVDQVSSSP QWNWRVRSVANV AQLHPTTLVKHK TSYRPPLNVCQD QSHSLFYPHPYG N-P-V-E-(x)3, x-P-E-F--G-S-x(2), K-x(2)-F-P-Q-x-T, L-x-A-x-E-T-x 73 Phage display (common panning) 3 PMID:28167275 Serum antibodies Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) We synthesize identified peptides in the array format and rescreen the serum used for phage panning to validate antibody binding peptides. Finally, we systematically vary the sequence of validated antibody binding peptides to identify those amino acids within the peptides that are crucial for binding "their" antibody species. The resulting immune fingerprints can then be used to trace them back to potential antigens. We investigated the serum of an individual in this pipeline, which led to the identification of 73 antibody fingerprints. Some fingerprints could be traced back to their most likely antigen, for example the immunodominant capsid protein VP1 of enteroviruses, most likely elicited by the ubiquitous poliovirus vaccination. 3117 NVRPRICRVRKWTLCF PAKHLCLLAANRVRRSWQCL PRHKKCFRVLRACIEY SDTCWKFYRGWPRRCRSN HAWCFPGPSLWPRRCRNN KSWCRQGFWPIRCSTT GPWKLSFL GPWNYRSYKFWSKTAK AWPYQNWSFWTSRFSD NIPSIRDCIPIGCLQYAFWR KRACKHSHGIWCTKW 11 Phage display (common panning) 5 PMID:28043792 BDNF/NT-3 growth factors receptor (EC:2.7.10.1) Brain-derived neurotrophic factor, BDNF Not determined. Not determined. T7 phage display library After the phage panning against recombinant Fc-fused TrkB (TrkB-Fc), agonistic phages were directly screened against TrkB-expressing HEK293 cells. Through subsequent screening of the first-hit BM17 peptide (NVRPRICRVRKWTLCF)-derived focus library, we successfully obtained the BM17d99 peptide (KSLPRMCRVRKWRLCF), which had no sequence similarity with BDNF but had TrkB-binding capacity. We then synthesized a dimeric BM17d99 analog peptide that could phosphorylate or activate TrkB by facilitating receptor homodimerization. Treatment of TrkB-expressing HEK293 cells with the dimeric BM17d99 analog peptide significantly induced the phosphorylation of TrkB, suggesting that homodimerization of TrkB was enhanced by the dimeric peptide. 3118 RGDDWA(20)[1.66955 ± 0.85] RGDDWE(12)[1.10951 ± 0.85] NRASNR(4)[2.21998 ± 0.85] KKILH*(4)[NT] 4 Phage display (common panning) 4 PMID:16787913 Kappa fractions of polyclonal immunoglobulin G(IgG) of multiplemyeloma patient MM077 Fibronectin(FN) Not determined. Not determined. X6 T7 phage display library ELISA The binding activities of phage clones to the Lactoferrin (LF) were measured by phage ELISA. The OD values at 450 nm were measured and data shown were reproduced from the Fig 1B in the reference. Two of the four peptides had the typical cell adhesion motif Arg-Gly-Asp (RGD), suggesting that human lactoferrin (hLF) may interact with RGD-containing proteins. Binding experiments using ELISA and surface plasmon resonance (SPR) analysis demonstrated that hLF bound to human fibronectin (hFN) and vitronectin (hVN) with relatively high affinity. Furthermore, the cell adhesion of Chinese hamster ovary (CHO), HeLa, and RAW cells to hFN or hVN coated on the culture plate was inhibited by hLF in a concentration-dependent manner, indicating that hLF interfered the cell adherent interaction through RGD motif. 3119 DVYWDTMAGSWITLTE ELPVDLEHEFQKMYME NDHQGHIKVTEYEVLG FEDLSPLLSKKSHTSS DFLDLTPLVGNAVMPV WQDTTAWFDNYREDTK SFTMYEPDQQTIVIES QSHIITMWRDLTIIDF HQVENGWWWMPHIDHN VDETVEWHDSNMELIH PVQSNKQYVPEPFVWM LDWKWEQLGSPLWTWN SDLVWDDLTPIF 13 Phage display (subtractive panning) 4 PMID:28028054 Kappa fractions mixture of polyclonal immunoglobulin G(IgG) of multiplemyeloma patient MM023 and MM031 and MM041 Not determined. Not determined. Not determined. X16 and X12 M13 phage display library The phage pool was pre-adsorbed on immobilized non-cognate mATG8 proteins. After the pre-adsorption, non-cognate mATG8 proteins was added to the phage pool and then transferred onto the selection plate. In the initial rounds of selections, input phage pools were additionally pre-adsorbed on immobilized GST alone. 3120 GVSNSENVEGAEGFLVY GKLRCENVEGKIHVAYN GVIQCYVPENVEGRSTA GVATSINENVEGYKPDY GNFMSKNVEGNPIVHFC GEVQCVFVPNVEGGEHD GLNQCARVPNVEGEHVD GDSQSKPKQQTCNVEGY GGAHSQNVEGRCSDKDY GYNQCNVEGQCYLNPCF GYYNSIDEANQYRTPCA GEEVSIDEALEKYRDFI GHKMSIDEAFPWEFFQY GIHWCKNEHKFYIDEAN GLIGSFETWGEIDEANY GYHGSTYESIDEAHFDF GEPLSTDEAITGRCHCF GGNFCIDEAQYQFVGPC GWEMCIDEACPCGHEVN GNDFSQTIDEAEYVYRD 20 Phage display (subtractive panning) 2 PMID:27906504 Serum of soy allergic patients Not determined. Not determined. Not determined. X16 phagemid library 3121 VAKYHGYPWNRRR[12 ± 11] LNRCVAKYHGYPWCRRR-NH2[6 ± 2] CVAKYHGYPWCRRR-NH2[5 ± 2] [VLW]-A-[KRL]-[YFW]-[HM]-G-x(2)-W 3 Phage display (competitive panning) 2 PMID:28039053 Dedicator of cytokinesis 2 (DOCK2) Not determined. Not determined. Not determined. CX7-10C T7 phage display library ELISA Biotinylated His-Avi-SUMO-TEV-DOCK2(1192-1622)was captured by the SA, and mixture of synthetic peptide and FLAG-His-TEV-Rac1(1-177) (2.5 nM) was added to the wells. IC50 values (nM) were calculated by Prism 5 (GraphPad Software, CA, USA). His-Avi-SUMOTEV-DOCK2(1192-1622) was immobilized to streptavidin (SA) M280 Dynabeads (Invitrogen, CA, USA) in PBS (045-29795, Wako) containing 0.5% BSA (blocking buffer). After washing in PBS containing 0.1% Tween 20 (PBST), beads were incubated with phage libraries for 1 h, and washed with PBST. Bound phages were competitively eluted by FLAG-His-TEV-Rac1(1-177) (1 mM) and were incubated with Escherichia coli BLT5615 cells (Merck) in logphase growth for phage amplification. These peptides inhibited DOCK2 activity at nanomolar concentrations and were delivered to intracellular compartments by combination with cell-penetrating peptide (CPP). Consequently, one peptide, R4-DCpep-2(V2W/K4R/ox)-NH2 (Ac-RRRRCWARYHGYPWCRRRR-NH2), inhibited migration in human B lymphocyte MINO cell line at IC50 = 120 nM. 3122 IQYRSWIPFSYP LDYRSWAPYATS YRSFDPWYPPVH LSIRSYTSPQWQ LNYRSYLPYETS YRSWxP 5 Phage display (common panning) 3/4 PMID:28035012 Viral protein 1 and 2 (VP1 and VP2) Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12) After biopanning, phage populations were sequenced and analyzed to identify a consensus peptide motif—YRSWXP. Two 12-mer peptides containing this sequence, NV-O-R5-3 (LDYRSWAPYATS) and NV-O-R5-6 (IQYRSWIPFSYP), were further characterized to evaluate the motif’s functional ability to detect VLPs and virus. Results indicated that these peptides effectively detect GI.1 VLPs in solidphase peptide arrays, ELISAs and dot blots. Further, their specificity for the S-domain of the major capsid protein enables them to detect a wide range of GI and GII norovirus genotypes. Both peptides were able to detect virus in norovirus-positive clinical stool samples. 3123 PPWYMCYPMKLKPDC[1000] RRCPLYISYDPVCRR[51] CMWWREICPVWW[65] 3 Phage display (subtractive panning) PMID:28153726 Recombinant V-Ki-ras2 Kirsten rat sarcoma viral oncogene homolog (K-Ras) with G12D substitution Not determined. Not determined. Not determined. CX7-10C T7 phage display library Surface plasmon resonance (SPR) To determine binding kinetics of peptides, an evaluation system using SPR was constructed.The KD value to KRas(G12D)in GDP form was shown in Table1. They thoroughly subtracted phages bound to WT K-Ras in the phage panning process. As a result, they successfully discovered K-Ras(G12D)-selective inhibitory peptides. 3124 GASESYL 1 Phage display (common panning) PMID:28208072 Anti-TIM polyclonal antibody Triosephosphate isomerase, TIM Not determined. Not determined. Ph.D.-7 phage display library (X7) A conformational epitope (A71G74S69D75T73F72V67) of TIM was confirmed by the phage display technology. 3125 YSTNWKNLSSLS(7) YSINWKNWLSKY(2) YSTNWKNQLSLS(1) YSMNWKNQLSLS(1) YSMNWKNQSSLY(1) 5 Phage display (common panning) 3 PMID:28272485 Anti-PRRSV monoclonal antibody A1 Not determined. Not determined. Not determined. Ph.D.-12 phage display library (X12)