                         SEQUENCE LISTING

<110>  Lehigh Univerity
       Pires, Marcos 
       Sabulski, Mary

<120>  BACTERIAL SURFACE HOMING MOIETIES CONJUGATED TO HAPTENS

<130>  030317-02 050118-01

<150>  US 62/665,495
<151>  2018-05-01

<150>  US 62/549,150
<151>  2017-08-23

<160>  6     

<170>  MS Word


<210>  1
<211>  37
<212>  PRT
<213>  Artificial Sequence

<220>  
<223>  Synthetic Sequence

<400>  1
       Leu Leu Gly Asp Phe Phe Arg Lys Ser Lys Glu Lys Ile Gly Lys Glu
       1               5                   10                  15
       Phe Lys Arg Ile Val Gln Arg Ile Lys Asp Phe Leu Arg Asn Leu Val
                   20                  25                  30
       Pro Arg Thr Glu Ser
               35

<210>  2
<211>  14
<212>  PRT
<213>  Artificial Sequence

<220>  
<223>  Synthetic Sequence

<400>  2
       Lys Leu Ala Lys Leu Ala Lys Lys Leu Ala Lys Leu Ala Lys
       1               5                   10                  
       Gly Cys Tyr


<210>  3
<211>  24
<212>  PRT
<213>  Artificial Sequence

<220> 
<223>  Synthetic Sequence

<400>  3
       Arg Arg Trp Val Arg Arg Val Arg Arg Trp Val Arg Arg Val Val Arg
       1               5                   10                  15
       Val Val Arg Arg Trp Val Arg Arg
                   20    
      

<210>  4
<211>  12
<212>  PRT
<213>  Artificial Sequence

<220>  
<223>  Synthetic Sequence

<400>  4
       Phe Trp Arg Gly Asp Leu Val Phe Asp Phe Gln Val
       1               5                   10 

<210>  5
<211>  12
<212>  PRT
<213>  Artificial Sequence

<220> 
<223>  Synthetic Sequence
<400>  5
       Ser Thr Gly Pro Cys Lys Thr Cys Thr Thr Pro Ala
       1               5                   10       

        
<210>  6
<211>  517
<212>  PRT
<213>  Artificial Sequence


<220> 
<223>  Synthetic Sequence
<400>  6
       Met Ser Asn Asn Thr Tyr Gln His Val Ser Asn Glu Ser Arg Tyr Val
       1               5                   10                  15 
       Lys Phe Asp Pro Thr Asp Thr Asn Phe Pro Pro Glu Ile Thr Asp Val
                   20                  25                  30
       Gln Ala Ala Ile Ala Ala Ile Ser Pro Ala Gly Val Asn Gly Val Pro 
               35                  40                  45        
       Asp Ala Ser Ser Thr Thr Lys Gly Ile Leu Phe Ile Pro Thr Glu Gln 
           50                  55                  60 
       Glu Val Ile Asp Gly Thr Asn Asn Thr Lys Ala Val Thr Pro Ala Thr
       65                  70                  75                  80 
       Leu Ala Thr Arg Leu Ser Tyr Pro Asn Ala Thr Glu Thr Val Tyr Gly
                       85                  90                  95
       Leu Thr Arg Tyr Ser Thr Asn Asp Glu Ala Ile Ala Gly Val Asn Asn 
                   100                 105                 110        
       Glu Ser Ser Ile Thr Pro Ala Lys Phe Thr Val Ala Leu Asn Asn Ala
               115                 120                 125  
       Phe Glu Thr Arg Val Ser Thr Glu Ser Ser Asn Gly Val Ile Lys Ile 
           130                 135                 140             
       Ser Ser Leu Pro Gln Ala Leu Ala Gly Ala Asp Asp Thr Thr Ala Met 
       145                 150                 155                 160
       Thr Pro Leu Lys Thr Gln Gln Leu Ala Ile Lys Leu Ile Ala Gln Ile 
                       165                 170                 175        
       Ala Pro Ser Glu Thr Thr Ala Thr Glu Ser Asp Gln Gly Val Val Gln
                   180                 185                 190  
       Leu Ala Thr Val Ala Gln Val Arg Gln Gly Thr Leu Arg Glu Gly Tyr 
               195                 200                 205                 
       Ala Ile Ser Pro Tyr Thr Phe Met Asn Ser Ser Ser Thr Glu Glu Tyr 
           210                 215                 220                 
       Lys Gly Val Ile Lys Leu Gly Thr Gln Ser Glu Val Asn Ser Asn Asn 
       225                 230                 235                 240        
       Ala Ser Val Ala Val Thr Gly Ala Thr Leu Asn Gly Arg Gly Ser Thr 
                       245                 250                 255  
       Thr Ser Met Arg Gly Val Val Lys Leu Thr Thr Thr Ala Gly Ser Gln
                   260                 265                 270                 
       Ser Gly Gly Asp Ala Ser Ser Ala Leu Ala Trp Asn Ala Asp Val Ile
               275                 280                 285                 
       Gln Gln Arg Gly Gly Gln Ile Ile Tyr Gly Thr Leu Arg Ile Glu Asp
           290                 295                 300                         
       Thr Phe Thr Ile Ala Asn Gly Gly Ala Asn Ile Thr Gly Thr Val Arg
       305                 310                 315                 320  
       Met Thr Gly Gly Tyr Ile Gln Gly Asn Arg Ile Val Thr Gln Asn Glu
                       325                 330                 335                 
       Ile Asp Arg Thr Ile Pro Val Gly Ala Ile Met Met Trp Ala Ala Asp
                  340                 345                 350                 
       Ser Leu Pro Ser Asp Ala Trp Arg Phe Cys His Gly Gly Thr Val Ser 
               355                 360                 365                 
       Ala Ser Asp Cys Pro Leu Tyr Ala Ser Arg Ile Gly Thr Arg Tyr Gly
           370                 375                 380                 
       Gly Asn Pro Ser Asn Pro Gly Leu Pro Asp Met Arg Gly Leu Phe Val
       385                 390                 395                 400                 
       Arg Gly Ser Gly Arg Gly Ser His Leu Thr Asn Pro Asn Val Asn Gly
                       405                 410                 415
       Asn Asp Gln Phe Gly Lys Pro Arg Leu Gly Val Gly Cys Thr Gly Gly 
                   410                 415                 420
       Tyr Val Gly Glu Val Gln Ile Gln Gln Met Ser Tyr His Lys His Ala 
               425                 430                 435        
       Gly Gly Phe Gly Glu His Asp Asp Leu Gly Ala Phe Gly Asn Thr Arg 
           440                 445                 450
       Arg Ser Asn Phe Val Gly Thr Arg Lys Gly Leu Asp Trp Asp Asn Arg
       455                 460                 465                 470
       Ser Tyr Phe Thr Asn Asp Gly Tyr Glu Ile Asp Pro Glu Ser Gln Arg
                       475                 480                 485
       Asn Ser Lys Tyr Thr Leu Asn Arg Pro Glu Leu Ile Gly Asn Glu Thr
                   490                 495                 500
       Arg Pro Trp Asn Ile Ser Leu Asn Tyr Ile Ile Lys Val Lys Glu 
               505                 510                 515        




  