Interaction of sperm with purified native chicken ZP1 and ZPC proteins

Nina Bausek; Hellin Ruckenbauer; Sabine Pfeifer; Wolfgang J Schneider; Franz Wohlrab

doi:10.1095/biolreprod.104.028605

Interaction of sperm with purified native chicken ZP1 and ZPC proteins

Nina Bausek
, Hellin Ruckenbauer
, Sabine Pfeifer
, Wolfgang J Schneider
, Franz Wohlrab

Research output: Journal article (peer-reviewed) › Journal article

33 Citations (Scopus)

Abstract

The avian perivitelline membrane (PVM) is the site of initial contact between sperm and egg. It consists of only two major components, which are both homologues of the mammalian zona pellucida (ZP) proteins, and belong to the ZP1 and ZPC families, respectively. We have established a method to isolate large quantities of both native avian ZP proteins and have used these preparations to investigate their sperm-binding capacities. Chicken ZPC forms multimeric structures of defined size and binds to an approximately 180-kDa protein complex present in rooster sperm extracts. Based on experiments using both PVM and isolated proteins, we show that chicken ZP1 is proteolytically degraded by a sperm-associated protease but that chicken ZPC remains intact. An antiserum directed against chicken ZP1 is capable of inhibiting sperm binding to the PVM. Taken together, these data suggest that ZP1, in addition to ZPC, plays a major role in the initial interactions between sperm and egg.

Original language	English
Pages (from-to)	684-690
Number of pages	7
Journal	Biology of Reproduction
Volume	71
Issue number	2
DOIs	https://doi.org/10.1095/biolreprod.104.028605
Publication status	Published - Aug 2004
Externally published	Yes

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title = "Interaction of sperm with purified native chicken ZP1 and ZPC proteins",

abstract = "The avian perivitelline membrane (PVM) is the site of initial contact between sperm and egg. It consists of only two major components, which are both homologues of the mammalian zona pellucida (ZP) proteins, and belong to the ZP1 and ZPC families, respectively. We have established a method to isolate large quantities of both native avian ZP proteins and have used these preparations to investigate their sperm-binding capacities. Chicken ZPC forms multimeric structures of defined size and binds to an approximately 180-kDa protein complex present in rooster sperm extracts. Based on experiments using both PVM and isolated proteins, we show that chicken ZP1 is proteolytically degraded by a sperm-associated protease but that chicken ZPC remains intact. An antiserum directed against chicken ZP1 is capable of inhibiting sperm binding to the PVM. Taken together, these data suggest that ZP1, in addition to ZPC, plays a major role in the initial interactions between sperm and egg.",

author = "Nina Bausek and Hellin Ruckenbauer and Sabine Pfeifer and Schneider, \{Wolfgang J\} and Franz Wohlrab",

year = "2004",

month = aug,

doi = "10.1095/biolreprod.104.028605",

language = "English",

volume = "71",

pages = "684--690",

journal = "Biology of Reproduction",

issn = "0006-3363",

publisher = "Oxford University Press",

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TY - JOUR

T1 - Interaction of sperm with purified native chicken ZP1 and ZPC proteins

AU - Bausek, Nina

AU - Ruckenbauer, Hellin

AU - Pfeifer, Sabine

AU - Schneider, Wolfgang J

AU - Wohlrab, Franz

PY - 2004/8

Y1 - 2004/8

N2 - The avian perivitelline membrane (PVM) is the site of initial contact between sperm and egg. It consists of only two major components, which are both homologues of the mammalian zona pellucida (ZP) proteins, and belong to the ZP1 and ZPC families, respectively. We have established a method to isolate large quantities of both native avian ZP proteins and have used these preparations to investigate their sperm-binding capacities. Chicken ZPC forms multimeric structures of defined size and binds to an approximately 180-kDa protein complex present in rooster sperm extracts. Based on experiments using both PVM and isolated proteins, we show that chicken ZP1 is proteolytically degraded by a sperm-associated protease but that chicken ZPC remains intact. An antiserum directed against chicken ZP1 is capable of inhibiting sperm binding to the PVM. Taken together, these data suggest that ZP1, in addition to ZPC, plays a major role in the initial interactions between sperm and egg.

AB - The avian perivitelline membrane (PVM) is the site of initial contact between sperm and egg. It consists of only two major components, which are both homologues of the mammalian zona pellucida (ZP) proteins, and belong to the ZP1 and ZPC families, respectively. We have established a method to isolate large quantities of both native avian ZP proteins and have used these preparations to investigate their sperm-binding capacities. Chicken ZPC forms multimeric structures of defined size and binds to an approximately 180-kDa protein complex present in rooster sperm extracts. Based on experiments using both PVM and isolated proteins, we show that chicken ZP1 is proteolytically degraded by a sperm-associated protease but that chicken ZPC remains intact. An antiserum directed against chicken ZP1 is capable of inhibiting sperm binding to the PVM. Taken together, these data suggest that ZP1, in addition to ZPC, plays a major role in the initial interactions between sperm and egg.

UR - https://www.scopus.com/pages/publications/3242772989

U2 - 10.1095/biolreprod.104.028605

DO - 10.1095/biolreprod.104.028605

M3 - Journal article

SN - 0006-3363

VL - 71

SP - 684

EP - 690

JO - Biology of Reproduction

JF - Biology of Reproduction

IS - 2

ER -

Interaction of sperm with purified native chicken ZP1 and ZPC proteins

Abstract

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