Structural Characterisation of Porcine Seminal Plasma Psp-IIPsp-1I
243
AQN1_PIG
AQN3_PIG
AWN_PIG
PSPI_PIG
PSPII_PIG
HSP7_HORSE
ASFP_BOVIN
AQN1_PIG
AQN3_PIG
AWN_PIG
PSPI_PIG
PSPII_PIG
HSP7_HORSE
AS FP_BOVIN
AQN1_PIG
AQN3_PIG
AWN_PIG
PSPI_PIG
PSPII_PIG
HSP7_HORSE
ASFP_BOVIN
1
10
20
30
40
50
1------- S-S --------1
1-- S-S
-AQNKGPHKCGGVLRDLSGRISTYEGPKTDCIWTILAKPGSRVFVAIPYLNLACGKEYVE
-AQNKGPDDCGGFLKNYSGWISYYKALTTNCVWTIEMKPGHKIILQILPLNLTCGKEYLE
-AWNRRSRSCGGVLRDPPGKIFNSDGPQKDCVWTIKVKPHFHVVLAIPPLNLSCGKEYVE
----LDYHACGGRLTDDYGTIFTYKGPKTECVWTLQVDPKYKLLVSIPTL~LTCGKEYVE
-ARINGPDECGRVIKDTSGSISNTDRQKNLCTWTILMKPDQKVRMAIPYLNLACGKEYVE
-AWNRRSRSCGGVLRDPPGKIFNSDGPQKDCVWTIKVKPHFHVVIAIPPLNLSCGKEYVE
MDWLPRNTNCGGILKEESGVIATYYGPKTNCVWTIQMPPEYHVRVSIQYLQLNCNKESLE
**
* *
* **
*
* * .. * *.** *
h
h
a h h
h h h h h
h
60
70
80
90
100
110
--------------1
VRDQRAGPDNFLKVCGGTGFVYQSSSNVATVKYSRDSHHPASSFNVYFYGIPQGAKA--LLDGPPGSEIIGKICGGISLVFRSSSNIATIKRLRTSGHRASPFHIYYYADPEGPLPFPY
VFDGLLSGPSYGKLCAGAAIVFLSTANTMTIKYNRISG~SSSPFLIFYGSSPGSEY---LLDGPPGSEIIGKICGGISLVFRSSSNIATIKYLRTSGQRASPFHIYYYADPEGPLPFPY
I IDGLPGSPVLGKICEGSLMDYRSSGSIMTVKYIREPEHPASFYEVLYFQDPQA-----* * *
* *
*
h
h
h h a
a h a
120
130
FERQTIIATEKNIP
FERQTIIATEKNIP
Fig_ 17.1. Comparison of the amino acid sequences of boar (AQN-l, AQN-3, AWN, PSP-I, and PSPII), stallion (HSP-7) and bull (aSFP) spermadhesin molecules. Absolutly conserved (*) and conservative amino acids (.) are labelled. The arrangement of the two disulphide bonds is indicated by S-S.
Glycosylated residues of PSP-I (Asn 50 ) and PSP-ll (Asn 9s ) are in boldface and doubly underlined. h
and a below the sequence alignment represent amino acid positions occupied in all CUB domains by
hydrophobic and aromatic residues, respectively, which display interior locations in the crystal structures of PSP-I/PSP-II and aSFP, and define the domain signature (Romero et aJ. 1997)
(1998) have provided evidence that neutral tri- and/or tetraantennary N-linked
carbohydrate chains of sow egg endo-~-galactosidase-treated zona pellucida glycoprotein ZPB with terminal Gal~(1-4)-GlcNAc sequences show homologous
sperm-binding activity. Hence, zona pellucida glycoproteins display both terminal and internal carbohydrate sequences that could act as spermadhesin
molecule-binding epitopes.
Boar spermadhesins are peripheral membrane proteins. As the external surface of the sperm plasma membrane undergoes continuous changes from spermatogenesis to fertilisation, the complex milieu of the ampullary-isthmic junction of the Fallopian tube, the place where presumably fertilisation in vivo takes
place, could induce remodelling of the sperm surface. Spermadhesin AWN has
been demonstrated by immunoelectron microscopy on remnants of the plasma-
243
AQN1_PIG
AQN3_PIG
AWN_PIG
PSPI_PIG
PSPII_PIG
HSP7_HORSE
ASFP_BOVIN
AQN1_PIG
AQN3_PIG
AWN_PIG
PSPI_PIG
PSPII_PIG
HSP7_HORSE
AS FP_BOVIN
AQN1_PIG
AQN3_PIG
AWN_PIG
PSPI_PIG
PSPII_PIG
HSP7_HORSE
ASFP_BOVIN
1
10
20
30
40
50
1------- S-S --------1
1-- S-S
-AQNKGPHKCGGVLRDLSGRISTYEGPKTDCIWTILAKPGSRVFVAIPYLNLACGKEYVE
-AQNKGPDDCGGFLKNYSGWISYYKALTTNCVWTIEMKPGHKIILQILPLNLTCGKEYLE
-AWNRRSRSCGGVLRDPPGKIFNSDGPQKDCVWTIKVKPHFHVVLAIPPLNLSCGKEYVE
----LDYHACGGRLTDDYGTIFTYKGPKTECVWTLQVDPKYKLLVSIPTL~LTCGKEYVE
-ARINGPDECGRVIKDTSGSISNTDRQKNLCTWTILMKPDQKVRMAIPYLNLACGKEYVE
-AWNRRSRSCGGVLRDPPGKIFNSDGPQKDCVWTIKVKPHFHVVIAIPPLNLSCGKEYVE
MDWLPRNTNCGGILKEESGVIATYYGPKTNCVWTIQMPPEYHVRVSIQYLQLNCNKESLE
**
* *
* **
*
* * .. * *.** *
h
h
a h h
h h h h h
h
60
70
80
90
100
110
--------------1
VRDQRAGPDNFLKVCGGTGFVYQSSSNVATVKYSRDSHHPASSFNVYFYGIPQGAKA--LLDGPPGSEIIGKICGGISLVFRSSSNIATIKRLRTSGHRASPFHIYYYADPEGPLPFPY
VFDGLLSGPSYGKLCAGAAIVFLSTANTMTIKYNRISG~SSSPFLIFYGSSPGSEY---LLDGPPGSEIIGKICGGISLVFRSSSNIATIKYLRTSGQRASPFHIYYYADPEGPLPFPY
I IDGLPGSPVLGKICEGSLMDYRSSGSIMTVKYIREPEHPASFYEVLYFQDPQA-----* * *
* *
*
h
h
h h a
a h a
120
130
FERQTIIATEKNIP
FERQTIIATEKNIP
Fig_ 17.1. Comparison of the amino acid sequences of boar (AQN-l, AQN-3, AWN, PSP-I, and PSPII), stallion (HSP-7) and bull (aSFP) spermadhesin molecules. Absolutly conserved (*) and conservative amino acids (.) are labelled. The arrangement of the two disulphide bonds is indicated by S-S.
Glycosylated residues of PSP-I (Asn 50 ) and PSP-ll (Asn 9s ) are in boldface and doubly underlined. h
and a below the sequence alignment represent amino acid positions occupied in all CUB domains by
hydrophobic and aromatic residues, respectively, which display interior locations in the crystal structures of PSP-I/PSP-II and aSFP, and define the domain signature (Romero et aJ. 1997)
(1998) have provided evidence that neutral tri- and/or tetraantennary N-linked
carbohydrate chains of sow egg endo-~-galactosidase-treated zona pellucida glycoprotein ZPB with terminal Gal~(1-4)-GlcNAc sequences show homologous
sperm-binding activity. Hence, zona pellucida glycoproteins display both terminal and internal carbohydrate sequences that could act as spermadhesin
molecule-binding epitopes.
Boar spermadhesins are peripheral membrane proteins. As the external surface of the sperm plasma membrane undergoes continuous changes from spermatogenesis to fertilisation, the complex milieu of the ampullary-isthmic junction of the Fallopian tube, the place where presumably fertilisation in vivo takes
place, could induce remodelling of the sperm surface. Spermadhesin AWN has
been demonstrated by immunoelectron microscopy on remnants of the plasma-